14gs
From Proteopedia
(New page: 200px<br /> <applet load="14gs" size="450" color="white" frame="true" align="right" spinBox="true" caption="14gs, resolution 2.80Å" /> '''GLUTATHIONE S-TRANS...) |
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| - | [[Image:14gs.gif|left|200px]]<br /> | + | [[Image:14gs.gif|left|200px]]<br /><applet load="14gs" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="14gs" size=" | + | |
caption="14gs, resolution 2.80Å" /> | caption="14gs, resolution 2.80Å" /> | ||
'''GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1'''<br /> | '''GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Three-dimensional structures of the apo form of human pi class glutathione | + | Three-dimensional structures of the apo form of human pi class glutathione transferase have been determined by X-ray crystallography. The structures suggest the enzyme recognizes its substrate, glutathione, by an induced-fit mechanism. Compared to complexed forms of the enzyme, the environment around the catalytic residue, Tyr 7, remains unchanged in the apoenzyme. This observation supports the view that Tyr 7 does not act as a general base in the reaction mechanism. The observed cooperativity of the dimeric enzyme may be due to the movements of a helix that forms one wall of the active site and, in particular, to movements of a tyrosine residue that is located in the subunit interface. |
==About this Structure== | ==About this Structure== | ||
| - | 14GS 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 MES 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] Full crystallographic information is available from [http:// | + | 14GS 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 <scene name='pdbligand=MES:'>MES</scene> 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=14GS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bello, M | + | [[Category: Bello, M Lo.]] |
[[Category: Federici, G.]] | [[Category: Federici, G.]] | ||
| - | [[Category: Oakley, A | + | [[Category: Oakley, A J.]] |
| - | [[Category: Parker, M | + | [[Category: Parker, M W.]] |
[[Category: Ricci, G.]] | [[Category: Ricci, G.]] | ||
[[Category: MES]] | [[Category: MES]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:38:20 2008'' |
Revision as of 09:38, 21 February 2008
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GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1
Overview
Three-dimensional structures of the apo form of human pi class glutathione transferase have been determined by X-ray crystallography. The structures suggest the enzyme recognizes its substrate, glutathione, by an induced-fit mechanism. Compared to complexed forms of the enzyme, the environment around the catalytic residue, Tyr 7, remains unchanged in the apoenzyme. This observation supports the view that Tyr 7 does not act as a general base in the reaction mechanism. The observed cooperativity of the dimeric enzyme may be due to the movements of a helix that forms one wall of the active site and, in particular, to movements of a tyrosine residue that is located in the subunit interface.
About this Structure
14GS is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.
Reference
Evidence for an induced-fit mechanism operating in pi class glutathione transferases., Oakley AJ, Lo Bello M, Ricci G, Federici G, Parker MW, Biochemistry. 1998 Jul 14;37(28):9912-7. PMID:9665696
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