1zof

From Proteopedia

Revision as of 05:27, 21 November 2007

Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter Pylori

Overview

The AhpC protein from H. pylori, a thioredoxin (Trx)-dependent alkyl, hydroperoxide-reductase, is a member of the ubiquitous 2-Cys, peroxiredoxins family (2-Cys Prxs), a group of thiol-specific antioxidant, enzymes. Prxs exert the protective antioxidant role in cells through their, peroxidase activity, whereby hydrogen peroxide, peroxynitrite and a wide, range of organic hydroperoxides (ROOH) are reduced and detoxified (ROOH +, 2e(-)-->ROH + H2O). In this study AhpC has been cloned and overexpressed, in E. coli. After purification to homogeneity, crystals of the recombinant, protein were grown. They diffract to 2.95 A resolution using synchrotron, radiation. The crystal structure of AhpC has been determined using the, molecular replacement method (R = 23.6%, R(free) = 25.9%). The model, similar in the overall to other members of the 2-Cys Prx family, crystallized as toroide-shaped complexes, consists of a pentameric, arrangement of homodimers [(alpha2)5 decamer]. The model of AhpC from H., pylori presents significant differences with respect to other members of, the family: apart from some loop regions, alpha5-helix and the C-terminus, is shifted, preventing the C-terminal tail of the second subunit from, extending toward this region of the molecule. Oligomerization properties, of AhpC have been also characterized by gel filtration chromatography.

About this Structure

1ZOF is a Single protein structure of sequence from Helicobacter pylori. Active as Peroxiredoxin, with EC number 1.11.1.15 Full crystallographic information is available from OCA.

Reference

Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter pylori., Papinutto E, Windle HJ, Cendron L, Battistutta R, Kelleher D, Zanotti G, Biochim Biophys Acta. 2005 Dec 1;1753(2):240-6. Epub 2005 Sep 21. PMID:16213196

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