2c3n
From Proteopedia
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(New page: 200px<br /> <applet load="2c3n" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c3n, resolution 1.50Å" /> '''HUMAN GLUTATHIONE-S...)
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Revision as of 16:51, 29 October 2007
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HUMAN GLUTATHIONE-S-TRANSFERASE T1-1, APO FORM
Overview
The crystal structures of wild-type human theta class, glutathione-S-transferase (GST) T1-1 and its W234R mutant, where Trp234, was replaced by Arg, were solved both in the presence and absence of, S-hexyl-glutathione. The W234R mutant was of interest due to its, previously observed enhanced catalytic activity compared to the wild-type, enzyme. GST T1-1 from rat and mouse naturally contain Arg in position 234, with correspondingly high catalytic efficiency. The overall structure of, GST T1-1 is similar to that of GST T2-2, as expected from their 53%, sequence identity at the protein level. Wild-type GST T1-1 has the, side-chain of Trp234 occupying a significant portion of the active site., This bulky residue prevents efficient binding of both glutathione and, hydrophobic substrates ... [(full description)]
About this Structure
2C3N is a [Single protein] structure of sequence from [Homo sapiens] with IOD as [ligand]. Active as [[1]], with EC number [2.5.1.18]. Full crystallographic information is available from [OCA].
Reference
Structural basis of the suppressed catalytic activity of wild-type human glutathione transferase T1-1 compared to its W234R mutant., Tars K, Larsson AK, Shokeer A, Olin B, Mannervik B, Kleywegt GJ, J Mol Biol. 2006 Jan 6;355(1):96-105. Epub 2005 Nov 8. PMID:16298388
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