期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 25, 期 6, 页码 531-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41594-018-0074-0
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资金
- Max Planck Society
- state of Thuringia [43-5572-321-12040-12]
- European Council under the European Union [615984]
- Studienstiftung des deutschen Volkes
- European Research Council (ERC) [615984] Funding Source: European Research Council (ERC)
The function of actin is coupled to the nucleotide bound to its active site. ATP hydrolysis is activated during polymerization; a delay between hydrolysis and inorganic phosphate (P-1) release results in a gradient of ATP, ADP-P ; and ADP along actin filaments (F-actin). Actin-binding proteins can recognize F-actin's nucleotide state, using it as a local 'age' tag. The underlying mechanism is complex and poorly understood. Here we report six high-resolution cryo-EM structures of F-actin from rabbit skeletal muscle in different nucleotide states. The structures reveal that actin polymerization repositions the proposed catalytic base, His161, closer to the gamma-phosphate. Nucleotide hydrolysis and P ; release modulate the conformational ensemble at the periphery of the filament, thus resulting in open and closed states, which can be sensed by coronin-1B. The drug-like toxin jasplakinolide locks F-actin in an open state. Our results demonstrate in detail how ATP hydrolysis links to F-actin's conformational dynamics and protein interaction.
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