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

被引:180
作者
Gajiwala, KS
Burley, SK
机构
[1] Rockefeller Univ, Lab Mol Biophys, New York, NY 10021 USA
[2] Rockefeller Univ, Howard Hughes Med Inst, New York, NY 10021 USA
关键词
HDEA; structure; function; acid resistance; stress response;
D O I
10.1006/jmbi.1999.3347
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
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.
引用
收藏
页码:605 / 612
页数:8
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