1eem
From Proteopedia
(New page: 200px<br /> <applet load="1eem" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eem, resolution 2.00Å" /> '''GLUTATHIONE TRANSFE...) |
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| - | [[Image:1eem.gif|left|200px]]<br /> | + | [[Image:1eem.gif|left|200px]]<br /><applet load="1eem" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1eem" size=" | + | |
caption="1eem, resolution 2.00Å" /> | caption="1eem, resolution 2.00Å" /> | ||
'''GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS'''<br /> | '''GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A new class of glutathione transferases has been discovered by analysis of | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1EEM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and GSH as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1EEM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GSH:'>GSH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EEM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Board, P.]] | [[Category: Board, P.]] | ||
[[Category: Chelvanayagam, G.]] | [[Category: Chelvanayagam, G.]] | ||
| - | [[Category: Chrunyk, B | + | [[Category: Chrunyk, B A.]] |
[[Category: Coggan, M.]] | [[Category: Coggan, M.]] | ||
| - | [[Category: Danley, D | + | [[Category: Danley, D E.]] |
[[Category: Easteal, S.]] | [[Category: Easteal, S.]] | ||
| - | [[Category: Gabel, C | + | [[Category: Gabel, C A.]] |
| - | [[Category: Geoghegan, K | + | [[Category: Geoghegan, K F.]] |
| - | [[Category: Griffor, M | + | [[Category: Griffor, M C.]] |
| - | [[Category: Hoth, L | + | [[Category: Hoth, L R.]] |
| - | [[Category: Jermiin, L | + | [[Category: Jermiin, L S.]] |
| - | [[Category: Kamath, A | + | [[Category: Kamath, A V.]] |
[[Category: Pandit, J.]] | [[Category: Pandit, J.]] | ||
| - | [[Category: Perregaux, D | + | [[Category: Perregaux, D E.]] |
| - | [[Category: Rosner, M | + | [[Category: Rosner, M H.]] |
| - | [[Category: Schulte, G | + | [[Category: Schulte, G K.]] |
[[Category: GSH]] | [[Category: GSH]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: putative oxidoreductase]] | [[Category: putative oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:54 2008'' |
Revision as of 10:26, 21 February 2008
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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.
About this Structure
1EEM is a Single protein structure of sequence from Homo sapiens with and as ligands. 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
Page seeded by OCA on Thu Feb 21 12:26:54 2008
Categories: Homo sapiens | Single protein | Board, P. | Chelvanayagam, G. | Chrunyk, B A. | Coggan, M. | Danley, D E. | Easteal, S. | Gabel, C A. | Geoghegan, K F. | Griffor, M C. | Hoth, L R. | Jermiin, L S. | Kamath, A V. | Pandit, J. | Perregaux, D E. | Rosner, M H. | Schulte, G K. | GSH | SO4 | Glutathione conjugating | Gst | Putative oxidoreductase
