期刊
STRUCTURE
卷 15, 期 5, 页码 553-564出版社
CELL PRESS
DOI: 10.1016/j.str.2007.03.010
关键词
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资金
- FIC NIH HHS [1 R01 TW007241-01] Funding Source: Medline
- NIAID NIH HHS [F32 AI 060300] Funding Source: Medline
- NIAMS NIH HHS [AR017346] Funding Source: Medline
- PHS HHS [D43 TE006230] Funding Source: Medline
Unlike processive cellular motors such as myosin V, whose structure has recently been determined in a rigor-like conformation, myosin II from contracting muscle filaments necessarily spends most of its time detached from actin. By using squid and sea scallop sources, however, we have now obtained similar rigor-like atomic structures for muscle myosin heads (S1). The significance of the hallmark closed actin-binding cleft in these crystal structures is supported here by actin/S1-binding studies. These structures reveal how different duty ratios, and hence cellular functions, of the myosin isoforms may be accounted for, in part, on the basis of detailed differences in interdomain contacts. Moreover, the rigor-like position of switch II turns out to be unique for myosin V. The overall arrangements of subdomains in the motor are relatively conserved in each of the known contractile states, and we explore qualitatively the energetics of these states.
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