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[[Image:1guk.gif|left|200px]]
[[Image:1guk.gif|left|200px]]


{{Structure
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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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}}


'''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: crystal structure]]
[[Category: Crystal structure]]
[[Category: glutathione s-transferase]]
[[Category: Glutathione s-transferase]]
[[Category: gst]]
[[Category: Gst]]
[[Category: oxidative stress]]
[[Category: Oxidative stress]]
[[Category: transferase]]
[[Category: Transferase]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:51:33 2008''

Revision as of 15:01, 2 May 2008

File:1guk.gif

Template:STRUCTURE 1guk

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

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