1dj8
From Proteopedia
CRYSTAL STRUCTURE OF E. COLI PERIPLASMIC PROTEIN HDEA
Structural highlights
Function[HDEA_ECOLI] Required for optimal acid stress protection. Exhibits a chaperone-like activity only at pH below 3 by suppressing non-specifically the aggregation of denaturated periplasmic proteins. Important for survival of enteric bacteria in the acidic environment of the host stomach. Also promotes the solubilization at neutral pH of proteins that had aggregated in their presence at acidic pHs. May cooperate with other periplasmic chaperones such as DegP and SurA.[1] [2] [3] [4] Publication Abstract from PubMedThe 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. HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria.,Gajiwala KS, Burley SK J Mol Biol. 2000 Jan 21;295(3):605-12. PMID:10623550[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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