HEADER GLUTATHIONE TRANSFERASE 07-JUN-93 2GST COMPND GLUTATHIONE S-TRANSFERASE (ISOENZYME 3-3) (E.C.2.5.1.18) COMPND 2 COMPLEX WITH (9S,10S)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10- COMPND 3 DIHROPHENANTHRENE SOURCE RAT (RATTUS RATTUS) LIVER AUTHOR X.JI,R.N.ARMSTRONG,G.L.GILLILAND REVDAT 1 31-OCT-93 2GST 0 JRNL AUTH X.JI,M.A.SESAY,L.DICKERT,S.M.PRASSAD,W.W.JOHNSON, JRNL AUTH 2 H.L.AMMON,R.N.ARMSTRONG,G.L.GILLILAND JRNL TITL STRUCTURE OF THE XENOBIOTIC SUBSTRATE BINDING JRNL TITL 2 SITE OF A GLUTATHIONE S-TRANSFERASE AS REVEALED JRNL TITL 3 BY X-RAY CRYSTALLOGRAPHIC ANALYSIS OF PRODUCT JRNL TITL 4 COMPLEXES WITH THE DIASTEREOMERS OF JRNL TITL 5 9-(S-GLUTATHIONYL)-10-HYDROXY-9, JRNL TITL 6 10-DIHYDROPHENANTHRENE JRNL REF TO BE PUBLISHED JRNL REFN 353 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH W.W.JOHNSON,S.LIU,X.JI,G.L.GILLILAND,R.N.ARMSTRONG REMARK 1 TITL TYROSINE 115 PARTICIPATES BOTH IN CHEMICAL AND REMARK 1 TITL 2 PHYSICAL STEPS OF THE CATALYTIC MECHANISM OF A REMARK 1 TITL 3 GLUTATHIONE S-TRANSFERASE REMARK 1 REF J.BIOL.CHEM. V. 268 11508 1993 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 REMARK 1 REFERENCE 2 REMARK 1 AUTH X.JI,P.ZHANG,R.N.ARMSTRONG,G.L.GILLILAND REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF A GLUTATHIONE REMARK 1 TITL 2 S-TRANSFERASE FROM THE MU GENE CLASS. STRUCTURAL REMARK 1 TITL 3 ANALYSIS OF THE BINARY COMPLEX OF ISOENZYME 3-3 REMARK 1 TITL 4 AND GLUTOTHIONE AT 2.2 ANGSTROMS RESOLUTION REMARK 1 REF BIOCHEMISTRY V. 31 10169 1992 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 REMARK 1 REFERENCE 3 REMARK 1 AUTH S.LIU,P.ZHANG,X.JI,W.W.JOHNSON,G.L.GILLILAND, REMARK 1 AUTH 2 R.N.ARMSTRONG REMARK 1 TITL CONTRIBUTION OF TYROSINE 6 TO THE CATALYTIC REMARK 1 TITL 2 MECHANISM OF ISOENZYME 3-3 OF GLUTATHIONE REMARK 1 TITL 3 S-TRANSFERASE REMARK 1 REF J.BIOL.CHEM. V. 267 4296 1992 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 REMARK 2 REMARK 2 RESOLUTION. 1.8 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM GPRLSA REMARK 3 AUTHORS FUREY,WANG,SAX REMARK 3 R VALUE 0.160 REMARK 3 RMSD BOND DISTANCES 0.020 ANGSTROMS REMARK 3 RMSD BOND ANGLE DISTANCES 0.035 ANGSTROMS REMARK 4 REMARK 4 SECONDARY STRUCTURE ASSIGNMENT IS ACCORDING TO KABSCH AND REMARK 4 SANDER (BIOPOLYMERS 22, 2577-2637, 1983), EXCEPT: REMARK 4 RESIDUES A 58 - A 61 (B 58 - B 61) AND A 204 - A 207 (B 204 REMARK 4 - B 207) WHICH FORM TWO CIS-PROLINE TURNS OF TYPE VIB. REMARK 5 REMARK 5 BETA-TURN TYPE ASSIGNMENT IS ACCORDING TO RICHARDSON REMARK 5 (ADVAN. PROTEIN. CHEM. 34, 167-339, 1981) AND WILMOT AND REMARK 5 THORNTON (J. MOL. BIOL. 203, 221-232, 1988). REMARK 6 REMARK 6 H5A AND H5B OF THE HELIX MAY BE CONSIDERED AS A SINGLE REMARK 6 LONG HELIX WHICH BENDS BY ABOUT 35 DEGREES. REMARK 7 REMARK 7 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL REMARK 7 YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO REMARK 7 CHAIN *A*, WHICH CORRESPONDS TO A ROTATION OF 179.749 REMARK 7 DEGREES AROUND THE DIRECTION 0.9536 -0.0553 0.2959. REMARK 8 REMARK 8 GPS IS (9S,10S)-9-(S-GLUTATHIOYL)-10-HYDROXY-9,10- REMARK 8 DIHYDROPHENANTHRENE. SEQRES 1 A 217 PRO MET ILE LEU GLY TYR TRP ASN VAL ARG GLY LEU THR SEQRES 2 A 217 HIS PRO ILE ARG LEU LEU LEU GLU TYR THR ASP SER SER SEQRES 3 A 217 TYR GLU GLU LYS ARG TYR ALA MET GLY ASP ALA PRO ASP SEQRES 4 A 217 TYR ASP ARG SER GLN TRP LEU ASN GLU LYS PHE LYS LEU SEQRES 5 A 217 GLY LEU ASP PHE PRO ASN LEU PRO TYR LEU ILE ASP GLY SEQRES 6 A 217 SER ARG LYS ILE THR GLN SER ASN ALA ILE MET ARG TYR SEQRES 7 A 217 LEU ALA ARG LYS HIS HIS LEU CYS GLY GLU THR GLU GLU SEQRES 8 A 217 GLU ARG ILE ARG ALA ASP ILE VAL GLU ASN GLN VAL MET SEQRES 9 A 217 ASP ASN ARG MET GLN LEU ILE MET LEU CYS TYR ASN PRO SEQRES 10 A 217 ASP PHE GLU LYS GLN LYS PRO GLU PHE LEU LYS THR ILE SEQRES 11 A 217 PRO GLU LYS MET LYS LEU TYR SER GLU PHE LEU GLY LYS SEQRES 12 A 217 ARG PRO TRP PHE ALA GLY ASP LYS VAL THR TYR VAL ASP SEQRES 13 A 217 PHE LEU ALA TYR ASP ILE LEU ASP GLN TYR HIS ILE PHE SEQRES 14 A 217 GLU PRO LYS CYS LEU ASP ALA PHE PRO ASN LEU LYS ASP SEQRES 15 A 217 PHE LEU ALA ARG PHE GLU GLY LEU LYS LYS ILE SER ALA SEQRES 16 A 217 TYR MET LYS SER SER ARG TYR LEU SER THR PRO ILE PHE SEQRES 17 A 217 SER LYS LEU ALA GLN TRP SER ASN LYS SEQRES 1 B 217 PRO MET ILE LEU GLY TYR TRP ASN VAL ARG GLY LEU THR SEQRES 2 B 217 HIS PRO ILE ARG LEU LEU LEU GLU TYR THR ASP SER SER SEQRES 3 B 217 TYR GLU GLU LYS ARG TYR ALA MET GLY ASP ALA PRO ASP SEQRES 4 B 217 TYR ASP ARG SER GLN TRP LEU ASN GLU LYS PHE LYS LEU SEQRES 5 B 217 GLY LEU ASP PHE PRO ASN LEU PRO TYR LEU ILE ASP GLY SEQRES 6 B 217 SER ARG LYS ILE THR GLN SER ASN ALA ILE MET ARG TYR SEQRES 7 B 217 LEU ALA ARG LYS HIS HIS LEU CYS GLY GLU THR GLU GLU SEQRES 8 B 217 GLU ARG ILE ARG ALA ASP ILE VAL GLU ASN GLN VAL MET SEQRES 9 B 217 ASP ASN ARG MET GLN LEU ILE MET LEU CYS TYR ASN PRO SEQRES 10 B 217 ASP PHE GLU LYS GLN LYS PRO GLU PHE LEU LYS THR ILE SEQRES 11 B 217 PRO GLU LYS MET LYS LEU TYR SER GLU PHE LEU GLY LYS SEQRES 12 B 217 ARG PRO TRP PHE ALA GLY ASP LYS VAL THR TYR VAL ASP SEQRES 13 B 217 PHE LEU ALA TYR ASP ILE LEU ASP GLN TYR HIS ILE PHE SEQRES 14 B 217 GLU PRO LYS CYS LEU ASP ALA PHE PRO ASN LEU LYS ASP SEQRES 15 B 217 PHE LEU ALA ARG PHE GLU GLY LEU LYS LYS ILE SER ALA SEQRES 16 B 217 TYR MET LYS SER SER ARG TYR LEU SER THR PRO ILE PHE SEQRES 17 B 217 SER LYS LEU ALA GLN TRP SER ASN LYS FTNOTE 1 FTNOTE 1 RESIDUES 38, 60, AND 206 OF BOTH CHAINS ARE CIS PROLINES. HET GPS I 218 35 SEE REMARK 8 HET GPS J 218 35 SEE REMARK 8 HET SO4 U 1 5 SULFATE HET SO4 U 2 5 SULFATE FORMUL 3 GPS 2(C24 H29 N3 O7 S1) FORMUL 4 SO4 2(O4 S1) FORMUL 5 HOH *470(H2 O1) HELIX 1 H1A HIS A 14 TYR A 22 1 HELIX 2 H2A SER A 43 LEU A 46 1 HELIX 3 HA LYS A 49 LYS A 51 5 HELIX 4 H3A SER A 72 LYS A 82 1 HELIX 5 H4A GLU A 90 CYS A 114 1 HELIX 6 H5A PHE A 119 LYS A 128 1 HELIX 7 H5B ILE A 130 LEU A 141 1 HELIX 8 H6A TYR A 154 PHE A 169 1 HELIX 9 H7A PRO A 178 GLU A 188 1 HELIX 10 H8A LYS A 191 MET A 197 1 HELIX 11 H1B HIS B 14 TYR B 22 1 HELIX 12 H2B SER B 43 LEU B 46 1 HELIX 13 H3B SER B 72 LYS B 82 1 HELIX 14 H4B GLU B 90 CYS B 114 1 HELIX 15 H5 PHE B 119 LEU B 141 1 HELIX 16 H6B TYR B 154 PHE B 169 1 HELIX 17 H7B PRO B 178 GLU B 188 1 HELIX 18 H8B LYS B 191 MET B 197 1 SHEET 1 S1A 4 TYR A 27 TYR A 32 0 SHEET 2 S1A 4 MET A 2 TRP A 7 1 N GLU A 28 O MET A 2 SHEET 3 S1A 4 TYR A 61 ASP A 64 -1 N ILE A 3 O ILE A 63 SHEET 4 S1A 4 ARG A 67 THR A 70 -1 N ASP A 64 O ARG A 67 SHEET 1 S1B 4 TYR B 27 TYR B 32 0 SHEET 2 S1B 4 MET B 2 TRP B 7 1 N GLU B 28 O MET B 2 SHEET 3 S1B 4 TYR B 61 ASP B 64 -1 N ILE B 3 O ILE B 63 SHEET 4 S1B 4 ARG B 67 THR B 70 -1 N ASP B 64 O ARG B 67 TURN 1 1A ARG A 10 THR A 13 II' TURN 2 2A ASP A 36 ASP A 39 VIA TURN 3 4A ASN A 58 TYR A 61 VIB TURN 4 6A ASN A 116 PHE A 119 I TURN 5 7A LEU A 141 ARG A 144 II' TURN 6 8A GLU A 170 CYS A 173 I TURN 7 10A LEU A 174 PHE A 177 I TURN 8 11A SER A 199 TYR A 202 I TURN 9 12A SER A 204 ILE A 207 VIB TURN 10 13A SER A 209 ALA A 212 I TURN 11 1B ARG B 10 THR B 13 II' TURN 12 2B ASP B 36 ASP B 39 VIA TURN 13 3B GLU B 48 LYS B 51 I TURN 14 4B ASN B 58 TYR B 61 VIB TURN 15 6B ASN B 116 PHE B 119 I TURN 16 7B LEU B 141 ARG B 144 II' TURN 17 8B GLU B 170 CYS B 173 I TURN 18 10B LEU B 174 PHE B 177 I TURN 19 11B SER B 199 TYR B 202 I TURN 20 12B SER B 204 ILE B 207 VIB TURN 21 13B SER B 209 ALA B 212 I CRYST1 88.240 69.440 81.280 90.00 106.01 90.00 C 2 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.011333 0.000000 0.003252 0.00000 SCALE2 0.000000 0.014401 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012800 0.00000 MTRIX1 1 0.818800 -0.106700 0.564100 -6.34020 1 MTRIX2 1 -0.104100 -0.993900 -0.036900 31.80750 1 MTRIX3 1 0.564600 -0.028500 -0.824900 26.44790 1