Structure of a new crystal form of human Hsp70 ATPase domain

被引:40
作者
Osipiuk, J
Walsh, MA
Freeman, BC
Morimoto, RI
Joachimiak, A
机构
[1] Argonne Natl Lab, Ctr Mech Biol & Biotechnol, Argonne, IL 60439 USA
[2] Univ Gdansk, Dept Microbiol, PL-80822 Gdansk, Poland
[3] Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1999年 / 55卷
关键词
D O I
10.1107/S0907444999002103
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Hsp70 proteins are highly conserved proteins induced by heat shock and other stress conditions. An ATP-binding domain of human Hsp70 protein has been crystallized in two major morphological forms at pH 7.0 in the presence of PEG 8000 and CaCl2. Both crystal forms belong to the orthorhombic space group P2(1)2(1)2(1), but show no resemblance in unit-cell parameters. Analysis of the crystal structures for both forms shows a 1-2 Angstrom shift of one of the subdomains of the protein. This conformational change could reflect a 'natural' flexibility of the protein which might be relevant to ATP binding and may facilitate the interaction of other proteins with Hsp70 protein.
引用
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页码:1105 / 1107
页数:3
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