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16gs

From Proteopedia

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[[Image:16gs.gif|left|200px]]
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{{STRUCTURE_16gs| PDB=16gs | SCENE= }}
{{STRUCTURE_16gs| PDB=16gs | SCENE= }}
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'''GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3'''
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===GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9665696 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9665696}}
==About this Structure==
==About this Structure==
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[[Category: Detoxification]]
[[Category: Detoxification]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:32:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:34:42 2008''

Revision as of 12:34, 30 June 2008

Image:16gs.png

Template:STRUCTURE 16gs

GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3

Template:ABSTRACT PUBMED 9665696

About this Structure

16GS is a Single protein structure of sequence from Homo sapiens. 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

Page seeded by OCA on Mon Jun 30 15:34:42 2008

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