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The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites
Author(s) -
Zhao Yonghong,
Liu Deqian,
Kaluarachchi Warna D.,
Bellamy Henry D.,
White Mark A.,
Fox Robert O.
Publication year - 2003
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.03121403
Subject(s) - active site , dimer , catalytic triad , chemistry , chaperone (clinical) , escherichia coli , protein structure , crystal structure , hydrolase , stereochemistry , cofactor , binding site , multiple isomorphous replacement , heat shock protein , enzyme , crystallography , peptide sequence , biochemistry , organic chemistry , medicine , pathology , gene
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 Å resolution. YedU monomer has an α/β/α sandwich domain and a small α/β 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.