1eem: Difference between revisions

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[[Image:1eem.~~gif~~|left|200px]]

[[Image:1eem.png|left|200px]]

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~~'''~~GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS~~'''~~

===GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS===

~~==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.

The line below this paragraph, {{ABSTRACT_PUBMED_10783391}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10783391 is the PubMed ID number.

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==About this Structure==

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[[Category: Gst]]

[[Category: Putative oxidoreductase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 15~~:00:04 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:34:42 2008''

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-[[Image:1eem.gif|left|200px]]
+{{Seed}}
+[[Image:1eem.png|left|200px]]
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 {{STRUCTURE_1eem|  PDB=1eem  |  SCENE=  }}
-'''GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS'''
+===GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10783391}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10783391 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10783391}}
 ==About this Structure==
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 [[Category: Gst]]
 [[Category: Putative oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:00:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 00:34:42 2008''