HEADER CARBON-OXYGEN LYASE 13-NOV-90 4ENL 4ENL 2 COMPND ENOLASE (E.C.4.2.1.11) (2-PHOSPHO-*D-GLYCERATE HYDROLASE) 4ENL 3 COMPND 2 (HOLO) 4ENL 4 SOURCE BAKER'S YEAST (SACCHAROMYCES $CEREVISIAE) 4ENL 5 AUTHOR L.LEBIODA,B.STEC 4ENL 6 REVDAT 1 15-APR-92 4ENL 0 4ENL 7 JRNL AUTH L.LEBIODA,B.STEC 4ENL 8 JRNL TITL CRYSTAL STRUCTURE OF HOLOENZYME REFINED AT 1.9 4ENL 9 JRNL TITL 2 ANGSTROMS RESOLUTION: TRIGONAL-*BIPYRAMIDAL 4ENL 10 JRNL TITL 3 GEOMETRY OF THE CATION BINDING SITE 4ENL 11 JRNL REF J.AM.CHEM.SOC. V. 111 8511 1989 4ENL 12 JRNL REFN ASTM JACSAT US ISSN 0002-7863 004 4ENL 13 REMARK 1 4ENL 14 REMARK 1 REFERENCE 1 4ENL 15 REMARK 1 AUTH L.LEBIODA,B.STEC 4ENL 16 REMARK 1 TITL MECHANISM OF ENOLASE: THE CRYSTAL STRUCTURE OF 4ENL 17 REMARK 1 TITL 2 ENOLASE-*MG==2+==-*PHOSPHOGLYCERATE(SLASH) 4ENL 18 REMARK 1 TITL 3 PHOSPHOENOLPYRUVATE COMPLEX AT 2.2-*ANGSTROMS 4ENL 19 REMARK 1 TITL 4 RESOLUTION 4ENL 20 REMARK 1 REF BIOCHEMISTRY V. 30 2817 1991 4ENL 21 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 4ENL 22 REMARK 1 REFERENCE 2 4ENL 23 REMARK 1 AUTH L.LEBIODA,B.STEC,J.M.BREWER,E.TYKARSKA 4ENL 24 REMARK 1 TITL INHIBITION OF ENOLASE: THE CRYSTAL STRUCTURES OF 4ENL 25 REMARK 1 TITL 2 ENOLASE-*CA==2+==-*PHOSPHOGLYCERATE AND 4ENL 26 REMARK 1 TITL 3 ENOLASE-*ZN==2+==-*PHOSPHOGLYCOLATE COMPLEXES AT 4ENL 27 REMARK 1 TITL 2 2.2-*ANGSTROMS RESOLUTION 4ENL 28 REMARK 1 REF BIOCHEMISTRY V. 30 2823 1991 4ENL 29 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 4ENL 30 REMARK 1 REFERENCE 3 4ENL 31 REMARK 1 AUTH B.STEC,L.LEBIODA 4ENL 32 REMARK 1 TITL REFINED STRUCTURE OF YEAST APO-ENOLASE AT 2.25 4ENL 33 REMARK 1 TITL 2 ANGSTROMS RESOLUTION 4ENL 34 REMARK 1 REF J.MOL.BIOL. V. 211 235 1990 4ENL 35 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 4ENL 36 REMARK 1 REFERENCE 4 4ENL 37 REMARK 1 AUTH L.LEBIODA,B.STEC,J.M.BREWER 4ENL 38 REMARK 1 TITL THE STRUCTURE OF YEAST ENOLASE AT 2.25-*ANGSTROMS 4ENL 39 REMARK 1 TITL 2 RESOLUTION. AN 8-FOLD BETA+ALPHA-BARREL WITH A 4ENL 40 REMARK 1 TITL 3 NOVEL BETA BETA ALPHA ALPHA (BETA ALPHA)=6= 4ENL 41 REMARK 1 TITL 4 TOPOLOGY 4ENL 42 REMARK 1 REF J.BIOL.CHEM. V. 264 3685 1989 4ENL 43 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 4ENL 44 REMARK 1 REFERENCE 5 4ENL 45 REMARK 1 AUTH L.LEBIODA,B.STEC 4ENL 46 REMARK 1 TITL CRYSTAL STRUCTURE OF ENOLASE INDICATES THAT 4ENL 47 REMARK 1 TITL 2 ENOLASE AND PYRUVATE KINASE EVOLVED FROM A COMMON 4ENL 48 REMARK 1 TITL 3 ANCESTOR 4ENL 49 REMARK 1 REF NATURE V. 333 683 1988 4ENL 50 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 4ENL 51 REMARK 1 REFERENCE 6 4ENL 52 REMARK 1 AUTH L.LEBIODA,J.M.BREWER 4ENL 53 REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC 4ENL 54 REMARK 1 TITL 2 DATA FOR A TETRAGONAL FORM OF YEAST ENOLASE 4ENL 55 REMARK 1 REF J.MOL.BIOL. V. 180 213 1984 4ENL 56 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 4ENL 57 REMARK 2 4ENL 58 REMARK 2 RESOLUTION. 1.9 ANGSTROMS. 4ENL 59 REMARK 3 4ENL 60 REMARK 3 REFINEMENT. BY THE RESTRAINED LEAST SQUARES PROCEDURE OF J. 4ENL 61 REMARK 3 KONNERT AND W. HENDRICKSON (PROGRAM *PROLSQ*). THE R 4ENL 62 REMARK 3 VALUE IS 0.149. THE RMS DEVIATION FROM IDEALITY OF THE 4ENL 63 REMARK 3 BOND LENGTHS IS 0.015 ANGSTROMS. THE RMS DEVIATION FROM 4ENL 64 REMARK 3 IDEALITY OF THE BOND ANGLES IS 3.2 DEGREES. 4ENL 65 REMARK 4 4ENL 66 REMARK 4 IN THE PRESENCE OF MG++, ENOLASE IS A DIMER OF IDENTICAL 4ENL 67 REMARK 4 SUBUNITS. THE FOLLOWING CRYSTALLOGRAPHIC TWO-FOLD SYMMETRY 4ENL 68 REMARK 4 OPERATION 4ENL 69 REMARK 4 0.0 -1.0 0.0 124.1 4ENL 70 REMARK 4 -1.0 0.0 0.0 124.1 4ENL 71 REMARK 4 0.0 0.0 -1.0 66.9 4ENL 72 REMARK 4 WILL YIELD COORDINATES FOR THE SYMMETRY RELATED SUBUNIT 4ENL 73 REMARK 4 WHEN APPLIED TO THE COORDINATES IN THIS ENTRY. 4ENL 74 REMARK 5 4ENL 75 REMARK 5 RESIDUES GLY 41 - VAL 42 AND PRO 265 - LYS 269 ARE PROBABLY 4ENL 76 REMARK 5 PARTIALLY DISORDERED. 4ENL 77 REMARK 6 4ENL 78 REMARK 6 THE SHEET PRESENTED AS *BAR* ON SHEET RECORDS BELOW IS 4ENL 79 REMARK 6 ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS 4ENL 80 REMARK 6 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND 4ENL 81 REMARK 6 LAST STRANDS ARE IDENTICAL. THERE IS A SMALL STRAND BONDED 4ENL 82 REMARK 6 TO THE END OF STRAND 1 OF THE BARREL. THIS SMALL STRAND 4ENL 83 REMARK 6 STRAND AND STRAND 1 ARE PRESENTED AS SHEET S1. 4ENL 84 REMARK 7 4ENL 85 REMARK 7 THE RESIDUES PRESENTED ON *SITE ME1* RECORDS BELOW COMPRISE 4ENL 86 REMARK 7 THE METAL ION BINDING SITE (CONFORMATIONAL). THE RESIDUES 4ENL 87 REMARK 7 PRESENTED ON *SITE PHO* RECORDS BELOW COMPRISE THE 4ENL 88 REMARK 7 PHOSPHATE GROUP BINDING SITE. THE RESIDUES PRESENTED ON 4ENL 89 REMARK 7 *SITE CAT* RECORDS BELOW COMPRISE OTHER ACTIVE SITE 4ENL 90 REMARK 7 RESIDUES THAT ARE PROBABLY INVOLVED IN SUBSTRATE BINDING 4ENL 91 REMARK 7 AND CATALYSIS. 4ENL 92 SEQRES 1 436 ALA VAL SER LYS VAL TYR ALA ARG SER VAL TYR ASP SER 4ENL 93 SEQRES 2 436 ARG GLY ASN PRO THR VAL GLU VAL GLU LEU THR THR GLU 4ENL 94 SEQRES 3 436 LYS GLY VAL PHE ARG SER ILE VAL PRO SER GLY ALA SER 4ENL 95 SEQRES 4 436 THR GLY VAL HIS GLU ALA LEU GLU MET ARG ASP GLY ASP 4ENL 96 SEQRES 5 436 LYS SER LYS TRP MET GLY LYS GLY VAL LEU HIS ALA VAL 4ENL 97 SEQRES 6 436 LYS ASN VAL ASN ASP VAL ILE ALA PRO ALA PHE VAL LYS 4ENL 98 SEQRES 7 436 ALA ASN ILE ASP VAL SER ASP GLN LYS ALA VAL ASP ASP 4ENL 99 SEQRES 8 436 PHE LEU ILE SER LEU ASP GLY THR ALA ASN LYS SER LYS 4ENL 100 SEQRES 9 436 LEU GLY ALA ASN ALA ILE LEU GLY VAL SER LEU ALA ALA 4ENL 101 SEQRES 10 436 SER ARG ALA ALA ALA ALA GLU LYS ASN VAL PRO LEU TYR 4ENL 102 SEQRES 11 436 LYS HIS LEU ALA ASP LEU SER LYS SER LYS THR SER PRO 4ENL 103 SEQRES 12 436 TYR VAL LEU PRO VAL PRO PHE LEU ASN VAL LEU ASN GLY 4ENL 104 SEQRES 13 436 GLY SER HIS ALA GLY GLY ALA LEU ALA LEU GLN GLU PHE 4ENL 105 SEQRES 14 436 MET ILE ALA PRO THR GLY ALA LYS THR PHE ALA GLU ALA 4ENL 106 SEQRES 15 436 LEU ARG ILE GLY SER GLU VAL TYR HIS ASN LEU LYS SER 4ENL 107 SEQRES 16 436 LEU THR LYS LYS ARG TYR GLY ALA SER ALA GLY ASN VAL 4ENL 108 SEQRES 17 436 GLY ASP GLU GLY GLY VAL ALA PRO ASN ILE GLN THR ALA 4ENL 109 SEQRES 18 436 GLU GLU ALA LEU ASP LEU ILE VAL ASP ALA ILE LYS ALA 4ENL 110 SEQRES 19 436 ALA GLY HIS ASP GLY LYS VAL LYS ILE GLY LEU ASP CYS 4ENL 111 SEQRES 20 436 ALA SER SER GLU PHE PHE LYS ASP GLY LYS TYR ASP LEU 4ENL 112 SEQRES 21 436 ASP PHE LYS ASN PRO ASN SER ASP LYS SER LYS TRP LEU 4ENL 113 SEQRES 22 436 THR GLY PRO GLN LEU ALA ASP LEU TYR HIS SER LEU MET 4ENL 114 SEQRES 23 436 LYS ARG TYR PRO ILE VAL SER ILE GLU ASP PRO PHE ALA 4ENL 115 SEQRES 24 436 GLU ASP ASP TRP GLU ALA TRP SER HIS PHE PHE LYS THR 4ENL 116 SEQRES 25 436 ALA GLY ILE GLN ILE VAL ALA ASP ASP LEU THR VAL THR 4ENL 117 SEQRES 26 436 ASN PRO LYS ARG ILE ALA THR ALA ILE GLU LYS LYS ALA 4ENL 118 SEQRES 27 436 ALA ASP ALA LEU LEU LEU LYS VAL ASN GLN ILE GLY THR 4ENL 119 SEQRES 28 436 LEU SER GLU SER ILE LYS ALA ALA GLN ASP SER PHE ALA 4ENL 120 SEQRES 29 436 ALA GLY TRP GLY VAL MET VAL SER HIS ARG SER GLY GLU 4ENL 121 SEQRES 30 436 THR GLU ASP THR PHE ILE ALA ASP LEU VAL VAL GLY LEU 4ENL 122 SEQRES 31 436 ARG THR GLY GLN ILE LYS THR GLY ALA PRO ALA ARG SER 4ENL 123 SEQRES 32 436 GLU ARG LEU ALA LYS LEU ASN GLN LEU LEU ARG ILE GLU 4ENL 124 SEQRES 33 436 GLU GLU LEU GLY ASP ASN ALA VAL PHE ALA GLY GLU ASN 4ENL 125 SEQRES 34 436 PHE HIS HIS GLY ASP LYS LEU 4ENL 126 FTNOTE 1 4ENL 127 FTNOTE 1 RESIDUES PRO 143 AND PRO 265 ARE CIS PROLINES. 4ENL 128 FTNOTE 2 4ENL 129 FTNOTE 2 RESIDUES GLY 41 - VAL 42 AND PRO 265 - LYS 269 ARE PROBABLY 4ENL 130 FTNOTE 2 PARTIALLY DISORDERED. 4ENL 131 HET ZN 438 1 ZINC ++ ION 4ENL 132 HET SO4 444 5 SULFATE 4ENL 133 FORMUL 2 ZN ZN1 ++ 4ENL 134 FORMUL 3 SO4 O4 S1 4ENL 135 FORMUL 4 HOH *348(H2 O1) 4ENL 136 HELIX 1 I LEU 62 ALA 79 1 BROKEN BY PRO 74 4ENL 137 HELIX 2 J GLN 86 ASP 97 1 4ENL 138 HELIX 3 K ALA 107 GLU 124 1 4ENL 139 HELIX 4 L LEU 129 LEU 136 1 4ENL 140 HELIX 5 A PHE 179 ARG 200 1 4ENL 141 HELIX 6 A10 ALA 203 GLY 206 5 4ENL 142 HELIX 7 B ALA 221 ALA 234 1 4ENL 143 HELIX 8 B10 SER 249 GLU 251 5 4ENL 144 HELIX 9 C GLY 275 ARG 288 1 4ENL 145 HELIX 10 D TRP 303 LYS 311 1 4ENL 146 HELIX 11 D10 ASP 320 THR 323 5 4ENL 147 HELIX 12 E PRO 327 GLU 335 1 4ENL 148 HELIX 13 E10 VAL 346 ILE 349 5 4ENL 149 HELIX 14 F LEU 352 ALA 364 1 4ENL 150 HELIX 15 G PHE 382 LEU 390 1 4ENL 151 HELIX 16 H SER 403 LEU 419 1 4ENL 152 SHEET 1 MEA 3 LYS 4 ASP 12 0 4ENL 153 SHEET 2 MEA 3 ASN 16 THR 25 -1 O THR 24 N LYS 4 4ENL 154 SHEET 3 MEA 3 VAL 29 VAL 34 -1 N VAL 34 O VAL 19 4ENL 155 SHEET 1 BAR 9 TYR 144 ASN 155 0 4ENL 156 SHEET 2 BAR 9 GLU 168 PRO 173 -1 O ILE 171 N LEU 151 4ENL 157 SHEET 3 BAR 9 VAL 241 ASP 246 -1 N LYS 242 O ALA 172 4ENL 158 SHEET 4 BAR 9 SER 293 GLU 295 1 O SER 293 N LEU 245 4ENL 159 SHEET 5 BAR 9 GLN 316 ALA 319 1 O GLN 316 N ILE 294 4ENL 160 SHEET 6 BAR 9 ASP 340 LYS 345 1 N ALA 341 O ILE 317 4ENL 161 SHEET 7 BAR 9 GLY 368 HIS 373 1 N GLY 368 O ASP 340 4ENL 162 SHEET 8 BAR 9 GLN 394 LYS 396 1 O GLN 394 N VAL 371 4ENL 163 SHEET 9 BAR 9 TYR 144 ASN 155 1 0 VAL 148 N ILE 395 4ENL 164 SHEET 1 S1 2 TYR 144 ASN 155 0 4ENL 165 SHEET 2 S1 2 ASN 422 PHE 425 1 O ASN 422 N TYR 144 4ENL 166 TURN 1 T1 ASP 12 GLY 15 TYPE I 4ENL 167 TURN 2 T2 THR 25 GLY 28 TYPE I 4ENL 168 TURN 3 T3 ALA 38 GLY 41 NON-BONDED 4ENL 169 TURN 4 T4 GLY 41 GLU 44 NON-BONDED 4ENL 170 TURN 5 T5 ASP 52 LYS 55 TYPE I 4ENL 171 TURN 6 T6 LYS 55 GLY 58 TYPE III' 4ENL 172 TURN 7 T7 TRP 56 LYS 59 TYPE III' 4ENL 173 TURN 8 T8 ASP 82 ASP 85 TYPE III 4ENL 174 TURN 9 T9 THR 99 LYS 102 NON-BONDED 4ENL 175 TURN 10 T10 SER 103 GLY 106 NON-BONDED 4ENL 176 TURN 11 T11 THR 141 TYR 144 NON-BONDED 4ENL 177 TURN 12 T12 ASN 152 ASN 155 BETA-BULGE 4ENL 178 TURN 13 T13 GLY 156 ALA 160 TYPE I 4ENL 179 TURN 14 T14 PRO 173 ALA 176 TYPE III 4ENL 180 TURN 15 T15 GLY 209 GLY 212 TYPE I 4ENL 181 TURN 16 T16 HIS 237 LYS 240 TYPE II 4ENL 182 TURN 17 T17 LYS 254 LYS 257 TYPE III' 4ENL 183 TURN 18 T18 ASP 259 PHE 262 TYPE I 4ENL 184 TURN 19 T19 ASP 268 LYS 271 TYPE I 4ENL 185 TURN 20 T20 LYS 287 PRO 290 NON-BONDED 4ENL 186 TURN 21 T21 ASP 296 ALA 299 NON-BONDED 4ENL 187 TURN 22 T22 ALA 299 ASP 302 TYPE I 4ENL 188 TURN 23 T23 THR 323 ASN 326 TYPE III' 4ENL 189 TURN 24 T24 PHE 363 GLY 366 TYPE I 4ENL 190 TURN 25 T25 ARG 374 GLU 377 NON-BONDED 4ENL 191 TURN 26 T26 LEU 419 ASN 422 TYPE II' 4ENL 192 TURN 27 T27 GLY 420 ALA 423 NON-BONDED 4ENL 193 TURN 28 T28 ALA 426 ASN 429 TYPE II' 4ENL 194 TURN 29 T29 PHE 430 HIS 431 TYPE I 4ENL 195 TURN 30 T20 HIS 432 LYS 435 TYPE III 4ENL 196 TURN 31 T21 GLY 433 LEU 436 TYPE I 4ENL 197 SITE 1 MEI 3 ASP 246 GLU 295 ASP 320 4ENL 198 SITE 1 PHO 1 ARG 374 4ENL 199 SITE 1 CAT 5 GLU 168 GLU 211 LYS 345 HIS 373 4ENL 200 SITE 2 CAT 5 LYS 396 4ENL 201 CRYST1 124.100 124.100 66.900 90.00 90.00 90.00 P 42 21 2 8 4ENL 202 ORIGX1 1.000000 0.000000 0.000000 0.00000 4ENL 203 ORIGX2 0.000000 1.000000 0.000000 0.00000 4ENL 204 ORIGX3 0.000000 0.000000 1.000000 0.00000 4ENL 205 SCALE1 0.008058 0.000000 0.000000 0.00000 4ENL 206 SCALE2 0.000000 0.008058 0.000000 0.00000 4ENL 207 SCALE3 0.000000 0.000000 0.014948 0.00000 4ENL 208