14gs

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[[Image:14gs.gif|left|200px]]
[[Image:14gs.gif|left|200px]]
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{{Structure
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|PDB= 14gs |SIZE=350|CAPTION= <scene name='initialview01'>14gs</scene>, resolution 2.80&Aring;
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The line below this paragraph, containing "STRUCTURE_14gs", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= GSTP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_14gs| PDB=14gs | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=14gs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=14gs OCA], [http://www.ebi.ac.uk/pdbsum/14gs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=14gs RCSB]</span>
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'''GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1'''
'''GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1'''
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[[Category: Parker, M W.]]
[[Category: Parker, M W.]]
[[Category: Ricci, G.]]
[[Category: Ricci, G.]]
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[[Category: apoenzyme]]
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[[Category: Apoenzyme]]
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[[Category: detoxification]]
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[[Category: Detoxification]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:30:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:28:14 2008''
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Revision as of 06:30, 2 May 2008

Image:14gs.gif

Template:STRUCTURE 14gs

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. 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 Fri May 2 09:30:41 2008

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