生物物理学
肽
伴侣(临床)
化学
蛋白质折叠
蛋白质结构
结合位点
结晶学
血浆蛋白结合
分子动力学
立体化学
生物化学
生物
医学
病理
计算化学
作者
Xiaotian Zhu,Xiaoliang Zhao,William F. Burkholder,Alexander Gragerov,Craig M. Ogata,Max E. Gottesman,Wayne A. Hendrickson
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:1996-06-14
卷期号:272 (5268): 1606-1614
被引量:1177
标识
DOI:10.1126/science.272.5268.1606
摘要
DnaK and other members of the 70-kilodalton heat-shock protein (hsp70) family promote protein folding, interaction, and translocation, both constitutively and in response to stress, by binding to unfolded polypeptide segments. These proteins have two functional units: a substrate-binding portion binds the polypeptide, and an adenosine triphosphatase portion facilitates substrate exchange. The crystal structure of a peptide complex with the substrate-binding unit of DnaK has now been determined at 2.0 Å resolution. The structure consists of a β-sandwich subdomain followed by α-helical segments. The peptide is bound to DnaK in an extended conformation through a channel defined by loops from the β sandwich. An α-helical domain stabilizes the complex, but does not contact the peptide directly. This domain is rotated in the molecules of a second crystal lattice, which suggests a model of conformation-dependent substrate binding that features a latch mechanism for maintaining long lifetime complexes.
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