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1guk
From Proteopedia
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[[Image:1guk.gif|left|200px]] | [[Image:1guk.gif|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF MURINE ALPHA-CLASS GSTA4-4''' | '''CRYSTAL STRUCTURE OF MURINE ALPHA-CLASS GSTA4-4''' | ||
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[[Category: Krengel, U.]] | [[Category: Krengel, U.]] | ||
[[Category: Schroter, K H.]] | [[Category: Schroter, K H.]] | ||
| - | [[Category: | + | [[Category: Crystal structure]] |
| - | [[Category: | + | [[Category: Glutathione s-transferase]] |
| - | [[Category: | + | [[Category: Gst]] |
| - | [[Category: | + | [[Category: Oxidative stress]] |
| - | [[Category: | + | [[Category: Transferase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:01:31 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:01, 2 May 2008
CRYSTAL STRUCTURE OF MURINE ALPHA-CLASS GSTA4-4
Overview
Glutathione S-transferases (GSTs) are ubiquitous multifunctional enzymes which play a key role in cellular detoxification. The enzymes protect the cells against toxicants by conjugating them to glutathione. Recently, a novel subgroup of alpha-class GSTs has been identified with altered substrate specificity which is particularly important for cellular defense against oxidative stress. Here, we report the crystal structure of murine GSTA4-4, which is the first structure of a prototypical member of this subgroup. The structure was solved by molecular replacement and refined to 2.9 A resolution. It resembles the structure of other members of the GST superfamily, but reveals a distinct substrate binding site.
About this Structure
1GUK is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a murine alpha-class glutathione S-transferase involved in cellular defense against oxidative stress., Krengel U, Schroter KH, Hoier H, Arkema A, Kalk KH, Zimniak P, Dijkstra BW, FEBS Lett. 1998 Feb 6;422(3):285-90. PMID:9498801 Page seeded by OCA on Fri May 2 18:01:31 2008
