| Literature DB >> 10623550 |
Abstract
The X-ray crystal structure of the Escherichia coli stress response protein HDEA has been determined at 2.0 A resolution. The single domain alpha-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. Copyright 2000 Academic Press.Entities:
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Year: 2000 PMID: 10623550 DOI: 10.1006/jmbi.1999.3347
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469