HEADER BIFUNCTIONAL(ISOMERASE AND SYNTHASE) 21-JUN-91 1PII 1PII 2 COMPND N-(5'PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE (E.C.5.3.1.24) 1PII 3 COMPND 2 COMPLEX WITH INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE 1PII 4 COMPND 3 (E.C.4.1.1.48) 1PII 5 SOURCE (ESCHERICHIA COLI) 1PII 6 AUTHOR M.WILMANNS,J.P.PRIESTLE,J.N.JANSONIUS 1PII 7 REVDAT 1 31-JAN-94 1PII 0 1PII 8 JRNL AUTH M.WILMANNS,J.P.PRIESTLE,T.NIERMANN,J.N.JANSONIUS 1PII 9 JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE BIFUNCTIONAL 1PII 10 JRNL TITL 2 ENZYME PHOSPHORIBOSYLANTHRANILATE ISOMERASE: 1PII 11 JRNL TITL 3 INDOLEGLYCEROLPHOSPHATE SYNTHASE FROM ESCHERICHIA 1PII 12 JRNL TITL 4 COLI REFINED AT 2.0 ANGSTROMS RESOLUTION 1PII 13 JRNL REF J.MOL.BIOL. V. 223 477 1992 1PII 14 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 1PII 15 REMARK 1 1PII 16 REMARK 1 REFERENCE 1 1PII 17 REMARK 1 AUTH M.WILMANNS,C.C.HYDE,D.R.DAVIES,K.KIRSCHNER, 1PII 18 REMARK 1 AUTH 2 J.N.JANSONIUS 1PII 19 REMARK 1 TITL STRUCTURAL CONSERVATION IN PARALLEL 1PII 20 REMARK 1 TITL 2 BETA(SLASH)ALPHA-*BARREL ENZYMES THAT CATALYZE 1PII 21 REMARK 1 TITL 3 THREE SEQUENTIAL REACTIONS IN THE PATHWAY OF 1PII 22 REMARK 1 TITL 4 TRYPTOPHAN BIOSYNTHESIS 1PII 23 REMARK 1 REF BIOCHEMISTRY V. 30 9161 1991 1PII 24 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 1PII 25 REMARK 1 REFERENCE 2 1PII 26 REMARK 1 AUTH J.P.PRIESTLE,M.G.GRUETTER,J.L.WHITE,M.G.VINCENT, 1PII 27 REMARK 1 AUTH 2 M.KANIA,E.WILSON,T.S.JARDETZKY,K.KIRSCHNER, 1PII 28 REMARK 1 AUTH 3 J.N.JANSONIUS 1PII 29 REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE BIFUNCTIONAL 1PII 30 REMARK 1 TITL 2 ENZYME N-(5'-PHOSPHORIBOSYL)ANTHRANILATE 1PII 31 REMARK 1 TITL 3 ISOMERASE-INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE 1PII 32 REMARK 1 TITL 4 FROM ESCHERICHIA COLI 1PII 33 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 84 5690 1987 1PII 34 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 1PII 35 REMARK 1 REFERENCE 3 1PII 36 REMARK 1 AUTH J.L.WHITE,M.G.GRUETTER,E.WILSON,C.THALLER,G.C.FORD, 1PII 37 REMARK 1 AUTH 2 J.D.G.SMIT,J.N.JANSONIUS,K.KIRSCHNER 1PII 38 REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY 1PII 39 REMARK 1 TITL 2 CRYSTALLOGRAPHIC DATA OF THE BIFUNCTIONAL ENZYME 1PII 40 REMARK 1 TITL 3 PHOSPHORIBOSYL-ANTHRANILATE 1PII 41 REMARK 1 TITL 4 ISOMERASE-INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE 1PII 42 REMARK 1 TITL 5 FROM ESCHERICHIA COLI 1PII 43 REMARK 1 REF /FEBS$ LETT. V. 148 87 1982 1PII 44 REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 165 1PII 45 REMARK 2 1PII 46 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. 1PII 47 REMARK 3 1PII 48 REMARK 3 REFINEMENT. 1PII 49 REMARK 3 PROGRAM 1 TNT 1PII 50 REMARK 3 AUTHORS 1 TRONRUD,TEN EYCK,MATTHEWS 1PII 51 REMARK 3 PROGRAM 2 X-PLOR 1PII 52 REMARK 3 AUTHORS 2 BRUNGER 1PII 53 REMARK 3 R VALUE 0.173 1PII 54 REMARK 3 RMSD BOND DISTANCES 0.010 ANGSTROMS 1PII 55 REMARK 3 RMSD BOND ANGLES 3.2 DEGREES 1PII 56 REMARK 3 RMSD TRIGONAL PLANARITY 0.008 ANGSTROMS 1PII 57 REMARK 3 RMSD PLANARITY 0.017 ANGSTROMS 1PII 58 REMARK 3 1PII 59 REMARK 3 NUMBER OF REFLECTIONS 44611 1PII 60 REMARK 3 RESOLUTION RANGE 15.0 - 2.0 ANGSTROMS 1PII 61 REMARK 3 1PII 62 REMARK 3 NUMBER OF PROTEIN ATOMS 3524 1PII 63 REMARK 3 NUMBER OF SOLVENT ATOMS 628 1PII 64 REMARK 4 1PII 65 REMARK 4 THIS BIFUNCTIONAL ENZYME CATALYZES TWO SEQUENTIAL STEPS OF 1PII 66 REMARK 4 THE TRYPTOPHAN BIOSYNTHETIC PATHWAY. THE TWO ACTIVE SITES 1PII 67 REMARK 4 ARE DISTINCT AND NONOVERLAPPING; RESIDUES 1 - 255 1PII 68 REMARK 4 CORRESPOND TO THE INDOLE-3-PHOSPHATE SYNTHASE DOMAIN. 1PII 69 REMARK 4 RESIDUES 256 - 452 CORRESPOND TO THE N-(5'PHOSPORIBOSYL) 1PII 70 REMARK 4 ANTHRANILATE ISOMERASE DOMAIN. 1PII 71 REMARK 5 1PII 72 REMARK 5 THE REFINED CRYSTAL STRUCTURE OF PRAI:IGPS INCLUDES TWO 1PII 73 REMARK 5 PHOSPHATE IONS, ONE BOUND TO EACH ACTIVE SITE OF THIS 1PII 74 REMARK 5 BIFUNCTIONAL ENZYME. 1PII 75 REMARK 6 1PII 76 REMARK 6 NOTE THAT SOME WATERS ARE DISTANT FROM THE PROTEIN AND MAY 1PII 77 REMARK 6 BELONG TO A SYMMETRY-RELATED MOLECULE. 1PII 78 REMARK 7 1PII 79 REMARK 7 RESIDUE 329 IS IDENTIFIED AS VAL IN PIR ENTRY GWEC. 1PII 80 REMARK 7 RECENT RESEQUENCING CONFIRMED THAT RESIDUE 329 IS ALA. IT 1PII 81 REMARK 7 IS PRESENTED AS ALA IN THIS ENTRY. 1PII 82 REMARK 8 1PII 83 REMARK 8 PRAI:IGPS CONSISTS OF TWO BETA/ALPHA-BARRELS, WHICH CAN BE 1PII 84 REMARK 8 SUPERIMPOSED ON EACH OTHER. IGPS HAS AN N-TERMINAL 1PII 85 REMARK 8 EXTENSION OUTSIDE OF THE BETA/ALPHA-BARREL, COMPRISING 1PII 86 REMARK 8 RESIDUES 1-48. 1PII 87 REMARK 9 1PII 88 REMARK 9 THE SECONDARY STRUCTURAL ELEMENTS (ALPHA-HELICES, 1PII 89 REMARK 9 BETA-STRANDS, TURNS) WERE DETERMINED WITH THE PROGRAM DSSP 1PII 90 REMARK 9 (KABSCH AND SANDER, 1983). 1PII 91 REMARK 10 1PII 92 REMARK 10 THE SHEET PRESENTED AS *I* ON SHEET RECORDS BELOW IS 1PII 93 REMARK 10 ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS 1PII 94 REMARK 10 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST 1PII 95 REMARK 10 AND LAST STRANDS ARE IDENTICAL. 1PII 96 REMARK 11 1PII 97 REMARK 11 THE SHEET PRESENTED AS *P* ON SHEET RECORDS BELOW IS 1PII 98 REMARK 11 ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS 1PII 99 REMARK 11 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST 1PII 100 REMARK 11 AND LAST STRANDS ARE IDENTICAL. 1PII 101 REMARK 12 1PII 102 REMARK 12 THE RESIDUES PRESENTED AS SITE *ASS* ON SITE RECORDS BELOW 1PII 103 REMARK 12 COMPRISE THE ACTIVE SITE OF IGPS. THE RESIDUES PRESENTED 1PII 104 REMARK 12 AS SITE *ASI* ON SITE RECORDS BELOW COMPRISE THE ACTIVE 1PII 105 REMARK 12 SITE OF PRAI. 1PII 106 REMARK 13 1PII 107 REMARK 13 THE FOLLOWING TRANSFORMATION BELOW WILL SUPERIMPOSE THE 1PII 108 REMARK 13 BETA/ALPHA-BARREL OF PRAI ON THE BETA/ALPHA-BARREL OF IGPS: 1PII 109 REMARK 13 1PII 110 REMARK 13 -0.333100 0.180850 -0.925390 34.278999 1PII 111 REMARK 13 0.597930 0.799370 -0.059000 -15.344000 1PII 112 REMARK 13 0.729060 -0.572970 -0.374410 -14.327000 1PII 113 REMARK 14 1PII 114 REMARK 14 SEQUENCE ADVISORY NOTICE: 1PII 115 REMARK 14 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1PII 116 REMARK 14 1PII 117 REMARK 14 SWISS-PROT ENTRY NAME:TRPC_ECOLI 1PII 118 REMARK 14 1PII 119 REMARK 14 SWISS-PROT RESIDUE PDB SEQRES 1PII 120 REMARK 14 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1PII 121 REMARK 14 ARG 94 GLN 94 1PII 122 REMARK 14 SER 319 VAL 319 1PII 123 REMARK 14 VAL 329 ALA 329 1PII 124 REMARK 14 THR 398 SER 398 1PII 125 SEQRES 1 452 MET GLN THR VAL LEU ALA LYS ILE VAL ALA ASP LYS ALA 1PII 126 SEQRES 2 452 ILE TRP VAL GLU ALA ARG LYS GLN GLN GLN PRO LEU ALA 1PII 127 SEQRES 3 452 SER PHE GLN ASN GLU VAL GLN PRO SER THR ARG HIS PHE 1PII 128 SEQRES 4 452 TYR ASP ALA LEU GLN GLY ALA ARG THR ALA PHE ILE LEU 1PII 129 SEQRES 5 452 GLU CYS LYS LYS ALA SER PRO SER LYS GLY VAL ILE ARG 1PII 130 SEQRES 6 452 ASP ASP PHE ASP PRO ALA ARG ILE ALA ALA ILE TYR LYS 1PII 131 SEQRES 7 452 HIS TYR ALA SER ALA ILE SER VAL LEU THR ASP GLU LYS 1PII 132 SEQRES 8 452 TYR PHE GLN GLY SER PHE ASN PHE LEU PRO ILE VAL SER 1PII 133 SEQRES 9 452 GLN ILE ALA PRO GLN PRO ILE LEU CYS LYS ASP PHE ILE 1PII 134 SEQRES 10 452 ILE ASP PRO TYR GLN ILE TYR LEU ALA ARG TYR TYR GLN 1PII 135 SEQRES 11 452 ALA ASP ALA CYS LEU LEU MET LEU SER VAL LEU ASP ASP 1PII 136 SEQRES 12 452 ASP GLN TYR ARG GLN LEU ALA ALA VAL ALA HIS SER LEU 1PII 137 SEQRES 13 452 GLU MET GLY VAL LEU THR GLU VAL SER ASN GLU GLU GLU 1PII 138 SEQRES 14 452 GLN GLU ARG ALA ILE ALA LEU GLY ALA LYS VAL VAL GLY 1PII 139 SEQRES 15 452 ILE ASN ASN ARG ASP LEU ARG ASP LEU SER ILE ASP LEU 1PII 140 SEQRES 16 452 ASN ARG THR ARG GLU LEU ALA PRO LYS LEU GLY HIS ASN 1PII 141 SEQRES 17 452 VAL THR VAL ILE SER GLU SER GLY ILE ASN THR TYR ALA 1PII 142 SEQRES 18 452 GLN VAL ARG GLU LEU SER HIS PHE ALA ASN GLY PHE LEU 1PII 143 SEQRES 19 452 ILE GLY SER ALA LEU MET ALA HIS ASP ASP LEU HIS ALA 1PII 144 SEQRES 20 452 ALA VAL ARG ARG VAL LEU LEU GLY GLU ASN LYS VAL CYS 1PII 145 SEQRES 21 452 GLY LEU THR ARG GLY GLN ASP ALA LYS ALA ALA TYR ASP 1PII 146 SEQRES 22 452 ALA GLY ALA ILE TYR GLY GLY LEU ILE PHE VAL ALA THR 1PII 147 SEQRES 23 452 SER PRO ARG CYS VAL ASN VAL GLU GLN ALA GLN GLU VAL 1PII 148 SEQRES 24 452 MET ALA ALA ALA PRO LEU GLN TYR VAL GLY VAL PHE ARG 1PII 149 SEQRES 25 452 ASN HIS ASP ILE ALA ASP VAL VAL ASP LYS ALA LYS VAL 1PII 150 SEQRES 26 452 LEU SER LEU ALA ALA VAL GLN LEU HIS GLY ASN GLU GLU 1PII 151 SEQRES 27 452 GLN LEU TYR ILE ASP THR LEU ARG GLU ALA LEU PRO ALA 1PII 152 SEQRES 28 452 HIS VAL ALA ILE TRP LYS ALA LEU SER VAL GLY GLU THR 1PII 153 SEQRES 29 452 LEU PRO ALA ARG GLU PHE GLN HIS VAL ASP LYS TYR VAL 1PII 154 SEQRES 30 452 LEU ASP ASN GLY GLN GLY GLY SER GLY GLN ARG PHE ASP 1PII 155 SEQRES 31 452 TRP SER LEU LEU ASN GLY GLN SER LEU GLY ASN VAL LEU 1PII 156 SEQRES 32 452 LEU ALA GLY GLY LEU GLY ALA ASP ASN CYS VAL GLU ALA 1PII 157 SEQRES 33 452 ALA GLN THR GLY CYS ALA GLY LEU ASP PHE ASN SER ALA 1PII 158 SEQRES 34 452 VAL GLU SER GLN PRO GLY ILE LYS ASP ALA ARG LEU LEU 1PII 159 SEQRES 35 452 ALA SER VAL PHE GLN THR LEU ARG ALA TYR 1PII 160 FTNOTE 1 1PII 161 FTNOTE 1 RESIDUES 380 - 388 HAVE VERY HIGH TEMPERATURE FACTORS. 1PII 162 HET PO4 453 5 PHOSPHATE GROUP 1PII 163 HET PO4 454 5 PHOSPHATE GROUP 1PII 164 FORMUL 2 PO4 2(O4 P1) 1PII 165 FORMUL 3 HOH *628(H2 O1) 1PII 166 HELIX 1 I0 VAL 4 GLN 22 1 1PII 167 HELIX 2 I1 PRO 70 TYR 77 1 1PII 168 HELIX 3 I2 PHE 97 ALA 107 1 RESIDUES 97-100: 3/10-HELIX 1PII 169 HELIX 4 I3 PRO 120 TYR 128 1 1PII 170 HELIX 5 I4 ASP 143 HIS 154 1 1PII 171 HELIX 6 I5 GLU 167 ALA 175 1 1PII 172 HELIX 7 I6 ASN 196 LEU 201 1 1PII 173 HELIX 8 I7 TYR 220 LEU 226 1 1PII 174 HELIX 9 I8' SER 237 MET 240 1 1PII 175 HELIX 10 I8 LEU 245 LEU 253 1 1PII 176 HELIX 11 P1 GLY 265 ALA 274 1 1PII 177 HELIX 12 P2 VAL 293 MET 300 1 1PII 178 HELIX 13 P3 ILE 316 LEU 326 1 1PII 179 HELIX 14 P4 GLN 339 ALA 348 1 1PII 180 HELIX 15 P6 TRP 391 LEU 394 5 1PII 181 HELIX 16 P7 CYS 413 ALA 417 1 1PII 182 HELIX 17 P8' SER 428 VAL 430 5 1PII 183 HELIX 18 P8 ALA 439 ARG 450 1 1PII 184 SHEET 1 I 9 ALA 49 CYS 54 0 1PII 185 SHEET 2 I 9 ALA 83 LEU 87 -1 N ALA 83 O PHE 50 1PII 186 SHEET 3 I 9 PRO 110 LYS 114 -1 O PRO 110 N ILE 84 1PII 187 SHEET 4 I 9 ALA 133 MET 137 -1 N ALA 133 O ILE 111 1PII 188 SHEET 5 I 9 GLY 159 VAL 164 -1 O GLY 159 N CYS 134 1PII 189 SHEET 6 I 9 VAL 180 ASN 184 -1 O VAL 180 N THR 162 1PII 190 SHEET 7 I 9 THR 210 GLU 214 -1 O THR 210 N VAL 181 1PII 191 SHEET 8 I 9 GLY 232 ILE 235 -1 N GLY 232 O VAL 211 1PII 192 SHEET 9 I 9 ALA 49 CYS 54 -1 N ILE 51 O PHE 233 1PII 193 SHEET 1 P 9 ASN 257 CYS 260 0 1PII 194 SHEET 2 P 9 TYR 278 ILE 282 -1 N TYR 278 O ASN 257 1PII 195 SHEET 3 P 9 GLN 306 PHE 311 -1 O GLN 306 N GLY 279 1PII 196 SHEET 4 P 9 ALA 330 LEU 333 -1 N ALA 330 O TYR 307 1PII 197 SHEET 5 P 9 ALA 354 SER 360 -1 O ALA 354 N VAL 331 1PII 198 SHEET 6 P 9 LYS 375 ASP 379 -1 O LYS 375 N LYS 357 1PII 199 SHEET 7 P 9 VAL 402 LEU 404 -1 N LEU 403 O TYR 376 1PII 200 SHEET 8 P 9 GLY 423 PHE 426 -1 O GLY 423 N LEU 404 1PII 201 SHEET 9 P 9 ASN 257 CYS 260 -1 N LYS 258 O LEU 424 1PII 202 TURN 1 I01 PRO 24 SER 27 1PII 203 TURN 2 I02 ALA 26 GLN 29 1PII 204 TURN 3 I03 PHE 28 GLU 31 1PII 205 TURN 4 I04 GLN 29 VAL 32 1PII 206 TURN 5 I05 HIS 38 ASP 41 1PII 207 TURN 6 I06 PHE 39 ALA 42 1PII 208 TURN 7 I07 ILE 76 HIS 79 1PII 209 TURN 8 I08 LYS 78 ALA 81 1PII 210 TURN 9 I09 ASP 119 GLN 122 1PII 211 TURN 10 I10 PRO 120 ILE 123 1PII 212 TURN 11 I11 ALA 126 TYR 129 1PII 213 TURN 12 I12 TYR 128 ALA 131 1PII 214 TURN 13 I13 MET 137 VAL 140 1PII 215 TURN 14 I14 HIS 154 GLU 157 1PII 216 TURN 15 I15 ILE 174 GLY 177 1PII 217 TURN 16 I16 ASP 187 ASP 190 1PII 218 TURN 17 I17 ASP 194 ARG 197 1PII 219 TURN 18 I18 LEU 195 THR 198 1PII 220 TURN 19 I19 ALA 202 LEU 205 1PII 221 TURN 20 I20 GLY 206 VAL 209 1PII 222 TURN 21 I21 GLU 225 HIS 228 1PII 223 TURN 22 I22 SER 227 ALA 230 1PII 224 TURN 23 I23 LEU 239 HIS 242 1PII 225 TURN 24 P01 VAL 284 SER 287 1PII 226 TURN 25 P02 SER 287 CYS 290 1PII 227 TURN 26 P03 VAL 299 ALA 302 1PII 228 TURN 27 P04 PRO 350 VAL 353 1PII 229 TURN 28 P05 ASP 390 LEU 393 1PII 230 TURN 29 P06 TRP 391 LEU 394 1PII 231 TURN 30 P07 LEU 394 GLN 397 1PII 232 TURN 31 P8A LEU 399 VAL 402 1PII 233 TURN 32 P8B GLY 409 ASN 412 1PII 234 TURN 33 P09 ALA 416 THR 419 1PII 235 TURN 34 P10 SER 428 GLU 431 1PII 236 TURN 35 P11 GLN 433 ILE 436 1PII 237 TURN 36 P12 GLN 447 ARG 450 1PII 238 TURN 37 P13 THR 448 ALA 451 1PII 239 SITE 1 ASS 24 VAL 4 LEU 5 ILE 8 GLU 53 1PII 240 SITE 2 ASS 24 LYS 55 SER 58 PRO 59 SER 60 1PII 241 SITE 3 ASS 24 LYS 61 TYR 92 PHE 93 LYS 114 1PII 242 SITE 4 ASS 24 PHE 116 GLU 163 ASN 184 ARG 186 1PII 243 SITE 5 ASS 24 LEU 188 LEU 191 GLU 214 SER 215 1PII 244 SITE 6 ASS 24 LEU 234 GLY 236 SER 237 ALA 238 1PII 245 SITE 1 ASI 19 LYS 258 CYS 260 ILE 282 ARG 289 1PII 246 SITE 2 ASI 19 VAL 291 VAL 310 GLN 332 HIS 334 1PII 247 SITE 3 ASI 19 ASP 379 SER 385 ALA 405 GLY 406 1PII 248 SITE 4 ASI 19 GLY 407 ASP 425 ASN 427 SER 428 1PII 249 SITE 5 ASI 19 ALA 429 VAL 430 GLU 431 1PII 250 CRYST1 104.700 104.700 68.000 90.00 90.00 90.00 P 41 4 1PII 251 ORIGX1 1.000000 0.000000 0.000000 0.00000 1PII 252 ORIGX2 0.000000 1.000000 0.000000 0.00000 1PII 253 ORIGX3 0.000000 0.000000 1.000000 0.00000 1PII 254 SCALE1 0.009551 0.000000 0.000000 0.00000 1PII 255 SCALE2 0.000000 0.009551 0.000000 0.00000 1PII 256 SCALE3 0.000000 0.000000 0.014706 0.00000 1PII 257 ATOM 1 N MET 1 33.386 0.895 46.670 1.00 39.14 1PII 258 ATOM 2 CA MET 1 33.925 1.649 45.559 1.00 30.88 1PII 259 ATOM 3 C MET 1 32.828 2.228 44.693 1.00 45.64 1PII 260 ATOM 4 O MET 1 31.759 1.642 44.558 1.00 54.61 1PII 261 ATOM 5 CB MET 1 34.804 0.802 44.618 1.00 45.33 1PII 262 ATHEADER BIFUNCTIONAL(ISOMERASE AND SYNTHASE) 21-JUN-91 1PII 1PII 2 COMPND N-(5'PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE (E.C.5.3.1.24) 1PII 3 COMPND 2 COMPLEX WITH INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE 1PII 4 COMPND 3 (E.C.4.1.1.48) 1PII 5 SOURCE (ESCHERICHIA COLI) 1PII 6 AUTHOR M.WILMANNS,J.P.PRIESTLE,J.N.JANSONIUS 1PII 7 REVDAT 1 31-JAN-94 1PII 0 1PII 8 JRNL AUTH M.WILMANNS,J.P.PRIESTLE,T.NIERMANN,J.N.JANSONIUS 1PII 9 JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE BIFUNCTIONAL 1PII 10 JRNL TITL 2 ENZYME PHOSPHORIBOSYLANTHRANILATE ISOMERASE: 1PII 11 JRNL TITL 3 INDOLEGLYCEROLPHOSPHATE SYNTHASE FROM ESCHERICHIA 1PII 12 JRNL TITL 4 COLI REFINED AT 2.0 ANGSTROMS RESOLUTION 1PII 13 JRNL REF J.MOL.BIOL. V. 223 477 1992 1PII 14 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 1PII 15 REMARK 1 1PII 16 REMARK 1 REFERENCE 1 1PII 17 REMARK 1 AUTH M.WILMANNS,C.C.HYDE,D.R.DAVIES,K.KIRSCHNER, 1PII 18 REMARK 1 AUTH 2 J.N.JANSONIUS 1PII 19 REMARK 1 TITL STRUCTURAL CONSERVATION IN PARALLEL 1PII 20 REMARK 1 TITL 2 BETA(SLASH)ALPHA-*BARREL ENZYMES THAT CATALYZE 1PII 21 REMARK 1 TITL 3 THREE SEQUENTIAL REACTIONS IN THE PATHWAY OF 1PII 22 REMARK 1 TITL 4 TRYPTOPHAN BIOSYNTHESIS 1PII 23 REMARK 1 REF BIOCHEMISTRY V. 30 9161 1991 1PII 24 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 1PII 25 REMARK 1 REFERENCE 2 1PII 26 REMARK 1 AUTH J.P.PRIESTLE,M.G.GRUETTER,J.L.WHITE,M.G.VINCENT, 1PII 27 REMARK 1 AUTH 2 M.KANIA,E.WILSON,T.S.JARDETZKY,K.KIRSCHNER, 1PII 28 REMARK 1 AUTH 3 J.N.JANSONIUS 1PII 29 REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE BIFUNCTIONAL 1PII 30 REMARK 1 TITL 2 ENZYME N-(5'-PHOSPHORIBOSYL)ANTHRANILATE 1PII 31 REMARK 1 TITL 3 ISOMERASE-INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE 1PII 32 REMARK 1 TITL 4 FROM ESCHERICHIA COLI 1PII 33 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 84 5690 1987 1PII 34 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 1PII 35 REMARK 1 REFERENCE 3 1PII 36 REMARK 1 AUTH J.L.WHITE,M.G.GRUETTER,E.WILSON,C.THALLER,G.C.FORD, 1PII 37 REMARK 1 AUTH 2 J.D.G.SMIT,J.N.JANSONIUS,K.KIRSCHNER 1PII 38 REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY 1PII 39 REMARK 1 TITL 2 CRYSTALLOGRAPHIC DATA OF THE BIFUNCTIONAL ENZYME 1PII 40 REMARK 1 TITL 3 PHOSPHORIBOSYL-ANTHRANILATE 1PII 41 REMARK 1 TITL 4 ISOMERASE-INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE 1PII 42 REMARK 1 TITL 5 FROM ESCHERICHIA COLI 1PII 43 REMARK 1 REF /FEBS$ LETT. V. 148 87 1982 1PII 44 REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 165 1PII 45 REMARK 2 1PII 46 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. 1PII 47 REMARK 3 1PII 48 REMARK 3 REFINEMENT. 1PII 49 REMARK 3 PROGRAM 1 TNT 1PII 50 REMARK 3 AUTHORS 1 TRONRUD,TEN EYCK,MATTHEWS 1PII 51 REMARK 3 PROGRAM 2 X-PLOR 1PII 52 REMARK 3 AUTHORS 2 BRUNGER 1PII 53 REMARK 3 R VALUE 0.173 1PII 54 REMARK 3 RMSD BOND DISTANCES 0.010 ANGSTROMS 1PII 55 REMARK 3 RMSD BOND ANGLES 3.2 DEGREES 1PII 56 REMARK 3 RMSD TRIGONAL PLANARITY 0.008 ANGSTROMS 1PII 57 REMARK 3 RMSD PLANARITY 0.017 ANGSTROMS 1PII 58 REMARK 3 1PII 59 REMARK 3 NUMBER OF REFLECTIONS 44611 1PII 60 REMARK 3 RESOLUTION RANGE 15.0 - 2.0 ANGSTROMS 1PII 61 REMARK 3 1PII 62 REMARK 3 NUMBER OF PROTEIN ATOMS 3524 1PII 63 REMARK 3 NUMBER OF SOLVENT ATOMS 628 1PII 64 REMARK 4 1PII 65 REMARK 4 THIS BIFUNCTIONAL ENZYME CATALYZES TWO SEQUENTIAL STEPS OF 1PII 66 REMARK 4 THE TRYPTOPHAN BIOSYNTHETIC PATHWAY. THE TWO ACTIVE SITES 1PII 67 REMARK 4 ARE DISTINCT AND NONOVERLAPPING; RESIDUES 1 - 255 1PII 68 REMARK 4 CORRESPOND TO THE INDOLE-3-PHOSPHATE SYNTHASE DOMAIN. 1PII 69 REMARK 4 RESIDUES 256 - 452 CORRESPOND TO THE N-(5'PHOSPORIBOSYL) 1PII 70 REMARK 4 ANTHRANILATE ISOMERASE DOMAIN. 1PII 71 REMARK 5 1PII 72 REMARK 5 THE REFINED CRYSTAL STRUCTURE OF PRAI:IGPS INCLUDES TWO 1PII 73 REMARK 5 PHOSPHATE IONS, ONE BOUND TO EACH ACTIVE SITE OF THIS 1PII 74 REMARK 5 BIFUNCTIONAL ENZYME. 1PII 75 REMARK 6 1PII 76 REMARK 6 NOTE THAT SOME WATERS ARE DISTANT FROM THE PROTEIN AND MAY 1PII 77 REMARK 6 BELONG TO A SYMMETRY-RELATED MOLECULE. 1PII 78 REMARK 7 1PII 79 REMARK 7 RESIDUE 329 IS IDENTIFIED AS VAL IN PIR ENTRY GWEC. 1PII 80 REMARK 7 RECENT RESEQUENCING CONFIRMED THAT RESIDUE 329 IS ALA. IT 1PII 81 REMARK 7 IS PRESENTED AS ALA IN THIS ENTRY. 1PII 82 REMARK 8 1PII 83 REMARK 8 PRAI:IGPS CONSISTS OF TWO BETA/ALPHA-BARRELS, WHICH CAN BE 1PII 84 REMARK 8 SUPERIMPOSED ON EACH OTHER. IGPS HAS AN N-TERMINAL 1PII 85 REMARK 8 EXTENSION OUTSIDE OF THE BETA/ALPHA-BARREL, COMPRISING 1PII 86 REMARK 8 RESIDUES 1-48. 1PII 87 REMARK 9 1PII 88 REMARK 9 THE SECONDARY STRUCTURAL ELEMENTS (ALPHA-HELICES, 1PII 89 REMARK 9 BETA-STRANDS, TURNS) WERE DETERMINED WITH THE PROGRAM DSSP 1PII 90 REMARK 9 (KABSCH AND SANDER, 1983). 1PII 91 REMARK 10 1PII 92 REMARK 10 THE SHEET PRESENTED AS *I* ON SHEET RECORDS BELOW IS 1PII 93 REMARK 10 ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS 1PII 94 REMARK 10 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST 1PII 95 REMARK 10 AND LAST STRANDS ARE IDENTICAL. 1PII 96 REMARK 11 1PII 97 REMARK 11 THE SHEET PRESENTED AS *P* ON SHEET RECORDS BELOW IS 1PII 98 REMARK 11 ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS 1PII 99 REMARK 11 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST 1PII 100 REMARK 11 AND LAST STRANDS ARE IDENTICAL. 1PII 101 REMARK 12 1PII 102 REMARK 12 THE RESIDUES PRESENTED AS SITE *ASS* ON SITE RECORDS BELOW 1PII 103 REMARK 12 COMPRISE THE ACTIVE SITE OF IGPS. THE RESIDUES PRESENTED 1PII 104 REMARK 12 AS SITE *ASI* ON SITE RECORDS BELOW COMPRISE THE ACTIVE 1PII 105 REMARK 12 SITE OF PRAI. 1PII 106 REMARK 13 1PII 107 REMARK 13 THE FOLLOWING TRANSFORMATION BELOW WILL SUPERIMPOSE THE 1PII 108 REMARK 13 BETA/ALPHA-BARREL OF PRAI ON THE BETA/ALPHA-BARREL OF IGPS: 1PII 109 REMARK 13 1PII 110 REMARK 13 -0.333100 0.180850 -0.925390 34.278999 1PII 111 REMARK 13 0.597930 0.799370 -0.059000 -15.344000 1PII 112 REMARK 13 0.729060 -0.572970 -0.374410 -14.327000 1PII 113 REMARK 14 1PII 114 REMARK 14 SEQUENCE ADVISORY NOTICE: 1PII 115 REMARK 14 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1PII 116 REMARK 14 1PII 117 REMARK 14 SWISS-PROT ENTRY NAME:TRPC_ECOLI 1PII 118 REMARK 14 1PII 119 REMARK 14 SWISS-PROT RESIDUE PDB SEQRES 1PII 120 REMARK 14 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1PII 121 REMARK 14 ARG 94 GLN 94 1PII 122 REMARK 14 SER 319 VAL 319 1PII 123 REMARK 14 VAL 329 ALA 329 1PII 124 REMARK 14 THR 398 SER 398 1PII 125 SEQRES 1 452 MET GLN THR VAL LEU ALA LYS ILE VAL ALA ASP LYS ALA 1PII 126 SEQRES 2 452 ILE TRP VAL GLU ALA ARG LYS GLN GLN GLN PRO LEU ALA 1PII 127 SEQRES 3 452 SER PHE GLN ASN GLU VAL GLN PRO SER THR ARG HIS PHE 1PII 128 SEQRES 4 452 TYR ASP ALA LEU GLN GLY ALA ARG THR ALA PHE ILE LEU 1PII 129 SEQRES 5 452 GLU CYS LYS LYS ALA SER PRO SER LYS GLY VAL ILE ARG 1PII 130 SEQRES 6 452 ASP ASP PHE ASP PRO ALA ARG ILE ALA ALA ILE TYR LYS 1PII 131 SEQRES 7 452 HIS TYR ALA SER ALA ILE SER VAL LEU THR ASP GLU LYS 1PII 132 SEQRES 8 452 TYR PHE GLN GLY SER PHE ASN PHE LEU PRO ILE VAL SER 1PII 133 SEQRES 9 452 GLN ILE ALA PRO GLN PRO ILE LEU CYS LYS ASP PHE ILE 1PII 134 SEQRES 10 452 ILE ASP PRO TYR GLN ILE TYR LEU ALA ARG TYR TYR GLN 1PII 135 SEQRES 11 452 ALA ASP ALA CYS LEU LEU MET LEU SER VAL LEU ASP ASP 1PII 136 SEQRES 12 452 ASP GLN TYR ARG GLN LEU ALA ALA VAL ALA HIS SER LEU 1PII 137 SEQRES 13 452 GLU MET GLY VAL LEU THR GLU VAL SER ASN GLU GLU GLU 1PII 138 SEQRES 14 452 GLN GLU ARG ALA ILE ALA LEU GLY ALA LYS VAL VAL GLY 1PII 139 SEQRES 15 452 ILE ASN ASN ARG ASP LEU ARG ASP LEU SER ILE ASP LEU 1PII 140 SEQRES 16 452 ASN ARG THR ARG GLU LEU ALA PRO LYS LEU GLY HIS ASN 1PII 141 SEQRES 17 452 VAL THR VAL ILE SER GLU SER GLY ILE ASN THR TYR ALA 1PII 142 SEQRES 18 452 GLN VAL ARG GLU LEU SER HIS PHE ALA ASN GLY PHE LEU 1PII 143 SEQRES 19 452 ILE GLY SER ALA LEU MET ALA HIS ASP ASP LEU HIS ALA 1PII 144 SEQRES 20 452 ALA VAL ARG ARG VAL LEU LEU GLY GLU ASN LYS VAL CYS 1PII 145 SEQRES 21 452 GLY LEU THR ARG GLY GLN ASP ALA LYS ALA ALA TYR ASP 1PII 146 SEQRES 22 452 ALA GLY ALA ILE TYR GLY GLY LEU ILE PHE VAL ALA THR 1PII 147 SEQRES 23 452 SER PRO ARG CYS VAL ASN VAL GLU GLN ALA GLN GLU VAL 1PII 148 SEQRES 24 452 MET ALA ALA ALA PRO LEU GLN TYR VAL GLY VAL PHE ARG 1PII 149 SEQRES 25 452 ASN HIS ASP ILE ALA ASP VAL VAL ASP LYS ALA LYS VAL 1PII 150 SEQRES 26 452 LEU SER LEU ALA ALA VAL GLN LEU HIS GLY ASN GLU GLU 1PII 151 SEQRES 27 452 GLN LEU TYR ILE ASP THR LEU ARG GLU ALA LEU PRO ALA 1PII 152 SEQRES 28 452 HIS VAL ALA ILE TRP LYS ALA LEU SER VAL GLY GLU THR 1PII 153 SEQRES 29 452 LEU PRO ALA ARG GLU PHE GLN HIS VAL ASP LYS TYR VAL 1PII 154 SEQRES 30 452 LEU ASP ASN GLY GLN GLY GLY SER GLY GLN ARG PHE ASP 1PII 155 SEQRES 31 452 TRP SER LEU LEU ASN GLY GLN SER LEU GLY ASN VAL LEU 1PII 156 SEQRES 32 452 LEU ALA GLY GLY LEU GLY ALA ASP ASN CYS VAL GLU ALA 1PII 157 SEQRES 33 452 ALA GLN THR GLY CYS ALA GLY LEU ASP PHE ASN SER ALA 1PII 158 SEQRES 34 452 VAL GLU SER GLN PRO GLY ILE LYS ASP ALA ARG LEU LEU 1PII 159 SEQRES 35 452 ALA SER VAL PHE GLN THR LEU ARG ALA TYR 1PII 160 FTNOTE 1 1PII 161 FTNOTE 1 RESIDUES 380 - 388 HAVE VERY HIGH TEMPERATURE FACTORS. 1PII 162 HET PO4 453 5 PHOSPHATE GROUP 1PII 163 HET PO4 454 5 PHOSPHATE GROUP 1PII 164 FORMUL 2 PO4 2(O4 P1) 1PII 165 FORMUL 3 HOH *628(H2 O1) 1PII 166 HELIX 1 I0 VAL 4 GLN 22 1 1PII 167 HELIX 2 I1 PRO 70 TYR 77 1 1PII 168 HELIX 3 I2 PHE 97 ALA 107 1 RESIDUES 97-100: 3/10-HELIX 1PII 169 HELIX 4 I3 PRO 120 TYR 128 1 1PII 170 HELIX 5 I4 ASP 143 HIS 154 1 1PII 171 HELIX 6 I5 GLU 167 ALA 175 1 1PII 172 HELIX 7 I6 ASN 196 LEU 201 1 1PII 173 HELIX 8 I7 TYR 220 LEU 226 1 1PII 174 HELIX 9 I8' SER 237 MET 240 1 1PII 175 HELIX 10 I8 LEU 245 LEU 253 1 1PII 176 HELIX 11 P1 GLY 265 ALA 274 1 1PII 177 HELIX 12 P2 VAL 293 MET 300 1 1PII 178 HELIX 13 P3 ILE 316 LEU 326 1 1PII 179 HELIX 14 P4 GLN 339 ALA 348 1 1PII 180 HELIX 15 P6 TRP 391 LEU 394 5 1PII 181 HELIX 16 P7 CYS 413 ALA 417 1 1PII 182 HELIX 17 P8' SER 428 VAL 430 5 1PII 183 HELIX 18 P8 ALA 439 ARG 450 1 1PII 184 SHEET 1 I 9 ALA 49 CYS 54 0 1PII 185 SHEET 2 I 9 ALA 83 LEU 87 -1 N ALA 83 O PHE 50 1PII 186 SHEET 3 I 9 PRO 110 LYS 114 -1 O PRO 110 N ILE 84 1PII 187 SHEET 4 I 9 ALA 133 MET 137 -1 N ALA 133 O ILE 111 1PII 188 SHEET 5 I 9 GLY 159 VAL 164 -1 O GLY 159 N CYS 134 1PII 189 SHEET 6 I 9 VAL 180 ASN 184 -1 O VAL 180 N THR 162 1PII 190 SHEET 7 I 9 THR 210 GLU 214 -1 O THR 210 N VAL 181 1PII 191 SHEET 8 I 9 GLY 232 ILE 235 -1 N GLY 232 O VAL 211 1PII 192 SHEET 9 I 9 ALA 49 CYS 54 -1 N ILE 51 O PHE 233 1PII 193 SHEET 1 P 9 ASN 257 CYS 260 0 1PII 194 SHEET 2 P 9 TYR 278 ILE 282 -1 N TYR 278 O ASN 257 1PII 195 SHEET 3 P 9 GLN 306 PHE 311 -1 O GLN 306 N GLY 279 1PII 196 SHEET 4 P 9 ALA 330 LEU 333 -1 N ALA 330 O TYR 307 1PII 197 SHEET 5 P 9 ALA 354 SER 360 -1 O ALA 354 N VAL 331 1PII 198 SHEET 6 P 9 LYS 375 ASP 379 -1 O LYS 375 N LYS 357 1PII 199 SHEET 7 P 9 VAL 402 LEU 404 -1 N LEU 403 O TYR 376 1PII 200 SHEET 8 P 9 GLY 423 PHE 426 -1 O GLY 423 N LEU 404 1PII 201 SHEET 9 P 9 ASN 257 CYS 260 -1 N LYS 258 O LEU 424 1PII 202 TURN 1 I01 PRO 24 SER 27 1PII 203 TURN 2 I02 ALA 26 GLN 29 1PII 204 TURN 3 I03 PHE 28 GLU 31 1PII 205 TURN 4 I04 GLN 29 VAL 32 1PII 206 TURN 5 I05 HIS 38 ASP 41 1PII 207 TURN 6 I06 PHE 39 ALA 42 1PII 208 TURN 7 I07 ILE 76 HIS 79 1PII 209 TURN 8 I08 LYS 78 ALA 81 1PII 210 TURN 9 I09 ASP 119 GLN 122 1PII 211 TURN 10 I10 PRO 120 ILE 123 1PII 212 TURN 11 I11 ALA 126 TYR 129 1PII 213 TURN 12 I12 TYR 128 ALA 131 1PII 214 TURN 13 I13 MET 137 VAL 140 1PII 215 TURN 14 I14 HIS 154 GLU 157 1PII 216 TURN 15 I15 ILE 174 GLY 177 1PII 217 TURN 16 I16 ASP 187 ASP 190 1PII 218 TURN 17 I17 ASP 194 ARG 197 1PII 219 TURN 18 I18 LEU 195 THR 198 1PII 220 TURN 19 I19 ALA 202 LEU 205 1PII 221 TURN 20 I20 GLY 206 VAL 209 1PII 222 TURN 21 I21 GLU 225 HIS 228 1PII 223 TURN 22 I22 SER 227 ALA 230 1PII 224 TURN 23 I23 LEU 239 HIS 242 1PII 225 TURN 24 P01 VAL 284 SER 287 1PII 226 TURN 25 P02 SER 287 CYS 290 1PII 227 TURN 26 P03 VAL 299 ALA 302 1PII 228 TURN 27 P04 PRO 350 VAL 353 1PII 229 TURN 28 P05 ASP 390 LEU 393 1PII 230 TURN 29 P06 TRP 391 LEU 394 1PII 231 TURN 30 P07 LEU 394 GLN 397 1PII 232 TURN 31 P8A LEU 399 VAL 402 1PII 233 TURN 32 P8B GLY 409 ASN 412 1PII 234 TURN 33 P09 ALA 416 THR 419 1PII 235 TURN 34 P10 SER 428 GLU 431 1PII 236 TURN 35 P11 GLN 433 ILE 436 1PII 237 TURN 36 P12 GLN 447 ARG 450 1PII 238 TURN 37 P13 THR 448 ALA 451 1PII 239 SITE 1 ASS 24 VAL 4 LEU 5 ILE 8 GLU 53 1PII 240 SITE 2 ASS 24 LYS 55 SER 58 PRO 59 SER 60 1PII 241 SITE 3 ASS 24 LYS 61 TYR 92 PHE 93 LYS 114 1PII 242 SITE 4 ASS 24 PHE 116 GLU 163 ASN 184 ARG 186 1PII 243 SITE 5 ASS 24 LEU 188 LEU 191 GLU 214 SER 215 1PII 244 SITE 6 ASS 24 LEU 234 GLY 236 SER 237 ALA 238 1PII 245 SITE 1 ASI 19 LYS 258 CYS 260 ILE 282 ARG 289 1PII 246 SITE 2 ASI 19 VAL 291 VAL 310 GLN 332 HIS 334 1PII 247 SITE 3 ASI 19 ASP 379 SER 385 ALA 405 GLY 406 1PII 248 SITE 4 ASI 19 GLY 407 ASP 425 ASN 427 SER 428 1PII 249 SITE 5 ASI 19 ALA 429 VAL 430 GLU 431 1PII 250 CRYST1 104.700 104.700 68.000 90.00 90.00 90.00 P 41 4 1PII 251 ORIGX1 1.000000 0.000000 0.000000 0.00000 1PII 252 ORIGX2 0.000000 1.000000 0.000000 0.00000 1PII 253 ORIGX3 0.000000 0.000000 1.000000 0.00000 1PII 254 SCALE1 0.009551 0.000000 0.000000 0.00000 1PII 255 SCALE2 0.000000 0.009551 0.000000 0.00000 1PII 256 SCALE3 0.000000 0.000000 0.014706 0.00000 1PII 257 ATOM 1 N MET 1 33.386 0.895 46.670 1.00 39.14 1PII 258 ATOM 2 CA MET 1 33.925 1.649 45.559 1.00 30.88 1PII 259 ATOM 3 C MET 1 32.828 2.228 44.693 1.00 45.64 1PII 260 ATOM 4 O MET 1 31.759 1.642 44.558 1.00 54.61 1PII 261 ATOM 5 CB MET 1 34.804 0.802 44.618 1.00 45.33 1PII 262 AT