1rq1

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Revision as of 23:40, 20 November 2007

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spinqualitylabelsall models 1rq1, resolution 2.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell

Overview

The flavoenzyme Ero1p produces disulfide bonds for oxidative protein, folding in the endoplasmic reticulum. Disulfides generated de novo within, Ero1p are transferred to protein disulfide isomerase and then to substrate, proteins by dithiol-disulfide exchange reactions. Despite this key role of, Ero1p, little is known about the mechanism by which this enzyme catalyzes, thiol oxidation. Here, we present the X-ray crystallographic structure of, Ero1p, which reveals the molecular details of the catalytic center, the, role of a CXXCXXC motif, and the spatial relationship between functionally, significant cysteines and the bound cofactor. Remarkably, the Ero1p active, site closely resembles that of the versatile thiol oxidase module of, Erv2p, a protein with no sequence homology to Ero1p. Furthermore, both, Ero1p and Erv2p display essential dicysteine motifs on mobile polypeptide, segments, suggesting that shuttling electrons to a rigid active site using, a flexible strand is a fundamental feature of disulfide-generating, flavoenzymes.

About this Structure

1RQ1 is a Single protein structure of sequence from Saccharomyces cerevisiae with CD, NEN and FAD as ligands. Full crystallographic information is available from OCA.

Reference

Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell., Gross E, Kastner DB, Kaiser CA, Fass D, Cell. 2004 May 28;117(5):601-10. PMID:15163408

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