1ons

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Revision as of 20:55, 20 November 2007

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spinqualitylabelsall models 1ons, resolution 2.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of Escherichia coli heat shock protein YedU

Overview

The mRNA of Escherichia coli yedU gene is induced 31-fold upon heat shock., The 31-kD YedU protein, also calls Hsp31, is highly conserved in several, human pathogens and has chaperone activity. We solved the crystal, structure of YedU at 2.2 A resolution. YedU monomer has an, alpha/beta/alpha sandwich domain and a small alpha/beta domain. YedU is a, dimer in solution, and its crystal structure indicates that a significant, amount of surface area is buried upon dimerization. There is an extended, hydrophobic patch that crosses the dimer interface on the surface of the, protein. This hydrophobic patch is likely the substrate-binding site, responsible for the chaperone activity. The structure also reveals a, potential protease-like catalytic triad composed of Cys184, His185, and, Asp213, although no enzymatic activity could be identified. YedU, coordinates a metal ion using His85, His122, and Glu90. This, 2-His-1-carboxylate motif is present in carboxypeptidase A (a zinc, enzyme), and a number of dioxygenases and hydroxylases that utilize iron, as a cofactor, suggesting another potential function for YedU.

About this Structure

1ONS is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Full crystallographic information is available from OCA.

Reference

The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites., Zhao Y, Liu D, Kaluarachchi WD, Bellamy HD, White MA, Fox RO, Protein Sci. 2003 Oct;12(10):2303-11. PMID:14500888

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