2c3n
From Proteopedia
(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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==About this Structure== | ==About this Structure== | ||
| - | 2C3N is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with IOD as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C3N OCA]]. | + | 2C3N is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with IOD as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C3N OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16298388 16298388] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16298388 16298388] | ||
| + | [[Category: Glutathione transferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:11:36 2007'' |
Revision as of 10:06, 30 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 [Glutathione transferase], with EC number [2.5.1.18]. Structure known Active Site: AC1. 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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