14gs: Difference between revisions
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[[Image:14gs.gif|left|200px]] | [[Image:14gs.gif|left|200px]] | ||
'''GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1''' | {{Structure | ||
|PDB= 14gs |SIZE=350|CAPTION= <scene name='initialview01'>14gs</scene>, resolution 2.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC ACID'>MES</scene> | |||
|ACTIVITY= [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] | |||
|GENE= GSTP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
14GS is a [ | 14GS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=14GS OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9665696 9665696] | ||
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:49:36 2008'' | ||
Revision as of 10:49, 20 March 2008
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| , resolution 2.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | GSTP1 (Homo sapiens) | ||||||
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1
OverviewOverview
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 StructureAbout this Structure
14GS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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