HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria

Ketan S. Gajiwala, Stephen K. Burley

Research output: Contribution to journalArticlepeer-review

176 Scopus citations

Abstract

The X-ray crystal structure of the Escherichia coli stress response protein HDEA has been determined at 2.0 Å resolution. The single domain α-helical protein is found in the periplasmic space, where it supports an acid resistance phenotype essential for infectivity of enteric bacterial pathogens, such as Shigella and E. coli. Functional studies demonstrate that HDEA is activated by a dimer-to-monomer transition at acidic pH, leading to suppression of aggregation by acid-denatured proteins. We suggest that HDEA may support chaperone-like functions during the extremely acidic conditions. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)605-612
Number of pages8
JournalJournal of molecular biology
Volume295
Issue number3
DOIs
StatePublished - Jan 21 2000
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

Keywords

  • Acid resistance
  • Function
  • HDEA
  • Stress response
  • Structure

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