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Protein Sci. 2003 Oct;12(10):2303-11.

The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites.

Author information

1
Department of Physiology and Biophysics, and The Graduate Program in Cellular Physiology and Molecular Biophysics, The University of Texas Medical Branch at Galveston, Galveston, Texas 77555, USA.

Abstract

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.

PMID:
14500888
PMCID:
PMC2366919
DOI:
10.1110/ps.03121403
[Indexed for MEDLINE]
Free PMC Article

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