3vln

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:25, 8 November 2023) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_3vln| PDB=3vln | SCENE= }}
 
-
===Human Glutathione Transferase O1-1 C32S Mutant in Complex with Ascorbic Acid===
 
-
{{ABSTRACT_PUBMED_22522127}}
 
-
==Function==
+
==Human Glutathione Transferase O1-1 C32S Mutant in Complex with Ascorbic Acid==
-
[[http://www.uniprot.org/uniprot/GSTO1_HUMAN GSTO1_HUMAN]] Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid.<ref>PMID:10783391</ref> <ref>PMID:11511179</ref> <ref>PMID:17226937</ref> <ref>PMID:18028863</ref> <ref>PMID:21106529</ref>
+
<StructureSection load='3vln' size='340' side='right'caption='[[3vln]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3vln]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VLN FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ASC:ASCORBIC+ACID'>ASC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3vln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vln OCA], [https://pdbe.org/3vln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vln RCSB], [https://www.ebi.ac.uk/pdbsum/3vln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vln ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/GSTO1_HUMAN GSTO1_HUMAN] Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid.<ref>PMID:10783391</ref> <ref>PMID:11511179</ref> <ref>PMID:17226937</ref> <ref>PMID:18028863</ref> <ref>PMID:21106529</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The reduction of dehydroascorbate (DHA) to ascorbic acid (AA) is a vital cellular function. The omega-class glutathione S-transferases (GSTs) catalyze several reductive reactions in cellular biochemistry, including DHA reduction. In humans, two isozymes (GSTO1-1 and GSTO2-2) with significant DHA reductase (DHAR) activity are found, sharing 64% sequence identity. While the activity of GSTO2-2 is higher, it is significantly more unstable in vitro. We report the first crystal structures of human GSTO2-2, stabilized through site-directed mutagenesis and determined at 1.9 A resolution in the presence and absence of glutathione (GSH). The structure of a human GSTO1-1 has been determined at 1.7 A resolution in complex with the reaction product AA, which unexpectedly binds in the G-site, where the glutamyl moiety of GSH binds. The structure suggests a similar mode of ascorbate binding in GSTO2-2. This is the first time that a non-GSH-based reaction product has been observed in the G-site of any GST. AA stacks against a conserved aromatic residue, F34 (equivalent to Y34 in GSTO2-2). Mutation of Y34 to alanine in GSTO2-2 eliminates DHAR activity. From these structures and other biochemical data, we propose a mechanism of substrate binding and catalysis of DHAR activity.
-
==About this Structure==
+
Structural Insights into the Dehydroascorbate Reductase Activity of Human Omega-Class Glutathione Transferases.,Zhou H, Brock J, Liu D, Board PG, Oakley AJ J Mol Biol. 2012 Apr 18. PMID:22522127<ref>PMID:22522127</ref>
-
[[3vln]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VLN OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<ref group="xtra">PMID:022522127</ref><references group="xtra"/><references/>
+
</div>
-
[[Category: Glutathione transferase]]
+
<div class="pdbe-citations 3vln" style="background-color:#fffaf0;"></div>
 +
 
 +
==See Also==
 +
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Board, P G.]]
+
[[Category: Large Structures]]
-
[[Category: Brock, J.]]
+
[[Category: Board PG]]
-
[[Category: Oakley, A J.]]
+
[[Category: Brock J]]
-
[[Category: Glutathione]]
+
[[Category: Oakley AJ]]
-
[[Category: Gst fold]]
+
-
[[Category: Reductase]]
+
-
[[Category: Transferase]]
+

Current revision

Human Glutathione Transferase O1-1 C32S Mutant in Complex with Ascorbic Acid

PDB ID 3vln

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3vln"
Personal tools