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6gsv

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Revision as of 15:52, 3 November 2021

FIRST-SPHERE AND SECOND-SPHERE ELECTROSTATIC EFFECTS IN THE ACTIVE SITE OF A CLASS MU GLUTATHIONE TRANSFERASE

Structural highlights

6gsv is a 2 chain structure with sequence from Black rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	CDNA INSERT OF CLONE PGT33MX (Black rat)
Activity:	Glutathione transferase, with EC number 2.5.1.18
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GSTM1_RAT] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The activation of the thiol of glutathione (GSH) bound in the active site of the class mu glutathione transferase M1-1 from rat involves a hydrogen-bonding network that includes a direct (first-sphere) interaction between the hydroxyl group of Y6 and the sulfur of GSH and second-sphere interactions involving a hydrogen bond between the main-chain amide N-H of L12 and the hydroxyl group of Y6 and an on-face hydrogen bond between the hydroxyl group of T13 and the pi-electron cloud of Y6 (i.e., T13-OH---pi-Y6-OH--- -SG). The functions of these hydrogen bonds have been examined with a combination of site-specific mutagenesis and X-ray crystallography. The hydroxyl group of Y6 has a normal pKa of about 10 even though it is shielded from solvent and is in a largely hydrophobic environment. The apparent pKa of GSH in the binary Y6F.GSH complex is increased by 1.6 log units, and the reactivity of the enzyme-bound nucleophile is reduced. The catalytic properties of the Y6L mutant are identical to those of Y6F, suggesting that the weakly polar on-edge interaction between the aromatic ring and sulfur has no influence on catalysis. The refined three-dimensional structure of the Y6F mutant in complex with GSH shows no major structural perturbation of the protein other than a change in the coordination environment of the sulfur. Removal of the second-sphere influence of the on-face hydrogen bond between the hydroxyl groups T13 as in the T13V and T13A mutants elevates the pKa of enzyme-bound GSH by about 0.7 pKa units. Crystal structures of these mutants show that structural changes in the active site are minor and suggest that the changes in pKa of E.GSH are due to the presence or absence of the on-face hydrogen bond. The T13S mutant has a completely different side-chain hydrogen-bonding geometry than T13 in the native enzyme and catalytic properties similar to the T13A and T13V mutants consistent with the absence of an on-face hydrogen bond. The gamma-methyl group of T13 is essential in enforcing the on-face hydrogen bond geometry and preventing the hydroxyl group from forming more favorable conventional hydrogen bonds.

First-sphere and second-sphere electrostatic effects in the active site of a class mu gluthathione transferase.,Xiao G, Liu S, Ji X, Johnson WW, Chen J, Parsons JF, Stevens WJ, Gilliland GL, Armstrong RN Biochemistry. 1996 Apr 16;35(15):4753-65. PMID:8664265^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Xiao G, Liu S, Ji X, Johnson WW, Chen J, Parsons JF, Stevens WJ, Gilliland GL, Armstrong RN. First-sphere and second-sphere electrostatic effects in the active site of a class mu gluthathione transferase. Biochemistry. 1996 Apr 16;35(15):4753-65. PMID:8664265 doi:http://dx.doi.org/10.1021/bi960189k

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6gsv"

@@ Line 1: / Line 1: @@
 ==FIRST-SPHERE AND SECOND-SPHERE ELECTROSTATIC EFFECTS IN THE ACTIVE SITE OF A CLASS MU GLUTATHIONE TRANSFERASE==
-<StructureSection load='6gsv' size='340' side='right' caption='[[6gsv]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+<StructureSection load='6gsv' size='340' side='right'caption='[[6gsv]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6gsv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Black_rat Black rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GSV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GSV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6gsv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Black_rat Black rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GSV FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GPS:L-GAMMA-GLUTAMYL-S-[(9S,10S)-10-HYDROXY-9,10-DIHYDROPHENANTHREN-9-YL]-L-CYSTEINYLGLYCINE'>GPS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GPS:L-GAMMA-GLUTAMYL-S-[(9S,10S)-10-HYDROXY-9,10-DIHYDROPHENANTHREN-9-YL]-L-CYSTEINYLGLYCINE'>GPS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDNA INSERT OF CLONE PGT33MX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10117 Black rat])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDNA INSERT OF CLONE PGT33MX ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10117 Black rat])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6gsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gsv OCA], [http://pdbe.org/6gsv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gsv RCSB], [http://www.ebi.ac.uk/pdbsum/6gsv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gsv ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6gsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gsv OCA], [https://pdbe.org/6gsv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gsv RCSB], [https://www.ebi.ac.uk/pdbsum/6gsv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gsv ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GSTM1_RAT GSTM1_RAT]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process.
+[[https://www.uniprot.org/uniprot/GSTM1_RAT GSTM1_RAT]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gs/6gsv_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gs/6gsv_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 32: / Line 32: @@
 ==See Also==
-*[[Glutathione S-transferase|Glutathione S-transferase]]
+*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
 == References ==
 <references/>
@@ Line 39: / Line 39: @@
 [[Category: Black rat]]
 [[Category: Glutathione transferase]]
+[[Category: Large Structures]]
 [[Category: Armstrong, R N]]
 [[Category: Gilliland, G L]]

6gsv

From Proteopedia

Revision as of 15:52, 3 November 2021

FIRST-SPHERE AND SECOND-SPHERE ELECTROSTATIC EFFECTS IN THE ACTIVE SITE OF A CLASS MU GLUTATHIONE TRANSFERASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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