14gs: Difference between revisions

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[[Image:14gs.gif|left|200px]]
{{Seed}}
[[Image:14gs.png|left|200px]]


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{{STRUCTURE_14gs|  PDB=14gs  |  SCENE=  }}  
{{STRUCTURE_14gs|  PDB=14gs  |  SCENE=  }}  


'''GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1'''
===GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_9665696}}, adds the Publication Abstract to the page
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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]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:30:41 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:30:57 2008''
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