1eem

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[[Image:1eem.gif|left|200px]]
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{{Seed}}
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[[Image:1eem.png|left|200px]]
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{{STRUCTURE_1eem| PDB=1eem | SCENE= }}
{{STRUCTURE_1eem| PDB=1eem | SCENE= }}
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'''GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS'''
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===GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS===
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==Overview==
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A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment. Glutathione S-transferases (GSTs) of the new class, named Omega, exist in several mammalian species and Caenorhabditis elegans. In humans, GSTO 1-1 is expressed in most tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities characteristic of the glutaredoxins. The structure of GSTO 1-1 has been determined at 2.0-A resolution and has a characteristic GST fold (Protein Data Bank entry code ). The Omega class GSTs exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit. Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione.
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The line below this paragraph, {{ABSTRACT_PUBMED_10783391}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 10783391 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10783391}}
==About this Structure==
==About this Structure==
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[[Category: Gst]]
[[Category: Gst]]
[[Category: Putative oxidoreductase]]
[[Category: Putative oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:00:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:34:42 2008''

Revision as of 21:34, 30 June 2008

Image:1eem.png

Template:STRUCTURE 1eem

GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS

Template:ABSTRACT PUBMED 10783391

About this Structure

1EEM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Identification, characterization, and crystal structure of the Omega class glutathione transferases., Board PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, Rosner MH, Chrunyk BA, Perregaux DE, Gabel CA, Geoghegan KF, Pandit J, J Biol Chem. 2000 Aug 11;275(32):24798-806. PMID:10783391

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