期刊
CYTOSKELETON
卷 67, 期 7, 页码 456-465出版社
WILEY
DOI: 10.1002/cm.20458
关键词
G-actin; F-actin; X-ray crystallography; conformational change
类别
资金
- Heart and Stroke Foundation of BC and Yukon
- Biomedical Research Council of A*STAR
- Canada Fdn. for Innovation
- Michael Smith Fdn. for Health Research
- Howard Hughes Medical Inst.
- CIHR
- National Research Program for Genomic Medicine
Heat shock proteins act as cytoplasmic chaperones to ensure correct protein folding and prevent protein aggregation. The presence of stoichiometric amounts of one such heat shock protein, Hsp27, in supersaturated solutions of unmodified G-actin leads to crystallization, in preference to polymerization, of the actin. Hsp27 is not evident in the resulting crystal structure. Thus, for the first time, we present the structure of G-actin in a form that is devoid of polymerization-deterring chemical modifications or binding partners, either of which may alter its conformation. The structure contains a calcium ion and ATP within a closed nucleotide-binding cleft, and the D-loop is disordered. This native G-actin structure invites comparison with the current F-actin model in order to understand the structural implications for actin polymerization. In particular, this analysis suggests a mechanism by which the bound cation coordinates conformational change and ATP-hydrolysis. (C) 2010 Wiley-Liss, Inc.
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