1bay: Difference between revisions

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[[Image:1bay.jpg|left|200px]]
{{Seed}}
[[Image:1bay.png|left|200px]]


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{{STRUCTURE_1bay|  PDB=1bay  |  SCENE=  }}  
{{STRUCTURE_1bay|  PDB=1bay  |  SCENE=  }}  


'''GLUTATHIONE S-TRANSFERASE YFYF CYS 47-CARBOXYMETHYLATED CLASS PI, FREE ENZYME'''
===GLUTATHIONE S-TRANSFERASE YFYF CYS 47-CARBOXYMETHYLATED CLASS PI, FREE ENZYME===




==Overview==
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The three-dimensional structure of mouse liver glutathione S-transferase P1-1 carboxymethylated at Cys-47 and its complex with S-(p-nitrobenzyl)glutathione have been determined by x-ray diffraction analysis. The structure of the modified enzyme described here is the first structural report for a Pi class glutathione S-transferase with no glutathione, glutathione S-conjugate, or inhibitor bound. It shows that part of the active site area, which includes helix alphaB and helix 310B, is disordered. However, the environment of Tyr-7, an essential residue for the catalytic reaction, remains unchanged. The position of the sulfur atom of glutathione is occupied in the ligand-free enzyme by a water molecule that is at H-bond distance from Tyr-7. We do not find any structural evidence for a tyrosinate form, and therefore our results suggest that Tyr-7 is not acting as a general base abstracting the proton from the thiol group of glutathione. The binding of the inhibitor S-(p-nitrobenzyl)-glutathione to the carboxymethylated enzyme results in a partial restructuring of the disordered area. The modification of Cys-47 sterically hinders structural organization of this region, and although it does not prevent glutathione binding, it significantly reduces the affinity. A detailed kinetic study of the modified enzyme indicates that the carboxymethylation increases the Km for glutathione by 3 orders of magnitude, although the enzyme can function efficiently under saturating conditions.
The line below this paragraph, {{ABSTRACT_PUBMED_9446594}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_9446594}}


==About this Structure==
==About this Structure==
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[[Category: Multigene family]]
[[Category: Multigene family]]
[[Category: Transferase]]
[[Category: Transferase]]
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