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

Yonghong Zhao, Deqian Liu, Warna D. Kaluarachchi, Henry D. Bellamy, Mark White, Robert O. Fox

Research output: Contribution to journalArticle

27 Scopus citations

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 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, His 122, 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.

Original languageEnglish (US)
Pages (from-to)2303-2311
Number of pages9
JournalProtein Science
Volume12
Issue number10
DOIs
StatePublished - Oct 1 2003

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Keywords

  • Catalytic triad
  • Chaperone
  • Hsp31
  • Metal binding protein
  • X-ray crystallography
  • YedU

ASJC Scopus subject areas

  • Biochemistry

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