12gs
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(New page: 200px<br /> <applet load="12gs" size="450" color="white" frame="true" align="right" spinBox="true" caption="12gs, resolution 2.10Å" /> '''GLUTATHIONE S-TRANS...)
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Revision as of 13:46, 12 November 2007
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GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-NONYL-GLUTATHIONE
Overview
Glutathione S -transferases (GSTs) play a pivotal role in the, detoxification of foreign chemicals and toxic metabolites. They were, originally termed ligandins because of their ability to bind large, molecules (molecular masses >400 Da), possibly for storage and transport, roles. The location of the ligandin site in mammalian GSTs is still, uncertain despite numerous studies in recent years. Here we show by X-ray, crystallography that the ligandin binding site in human pi class GST P1-1, occupies part of one of the substrate binding sites. This work has been, extended to the determination of a number of enzyme complex crystal, structures which show that very large ligands are readily accommodated, into this substrate binding site and in all, but one case, causes no, significant movement of protein side-chains. Some of these molecules make, use of a hitherto undescribed binding site located in a surface pocket of, the enzyme. This site is conserved in most, but not all, classes of GSTs, suggesting it may play an important functional role.
About this Structure
12GS is a Single protein structure of sequence from Homo sapiens with MES as ligand. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.
Reference
The ligandin (non-substrate) binding site of human Pi class glutathione transferase is located in the electrophile binding site (H-site)., Oakley AJ, Lo Bello M, Nuccetelli M, Mazzetti AP, Parker MW, J Mol Biol. 1999 Aug 27;291(4):913-26. PMID:10452896
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