HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria
HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria
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DOI：
10.1006/jmbi.1999.3347
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发表时间：
2000-01-21
影响因子：
5.6
通讯作者：
Burley, SK
中科院分区：
文献类型：
--
作者：
Gajiwala, KS;Burley, SK
大肠杆菌应激反应蛋白HDEA的X射线晶体结构已在2.0埃分辨率下确定。单结构域α-螺旋蛋白存在于周质空间中，在那里它支持对肠道细菌病原体如志贺氏菌和大肠杆菌的感染性所必需的耐酸性表型。杆菌功能研究表明，HDEA是激活的二聚体到单体的过渡在酸性pH值，导致抑制聚集的酸变性蛋白质。我们认为，HDEA可能支持分子伴侣样功能在极端酸性条件下。(C)北京大学出版社.
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.