期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 295, 期 3, 页码 605-612出版社
ACADEMIC PRESS LTD
DOI: 10.1006/jmbi.1999.3347
关键词
HDEA; structure; function; acid resistance; stress response
The X-ray crystal structure of the Escherichia coli stress response protein HDEA has been determined at 2.0 Angstrom 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. (C) 2000 Academic Press.
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