Rigor-like Structures from Muscle Myosins Reveal Key Mechanical Elements in the Transduction Pathways of This Allosteric Motor

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...

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Veröffentlicht in:Structure (London) 2007-05, Vol.15 (5), p.553-564
Hauptverfasser: Yang, Yuting, Gourinath, S., Kovács, Mihály, Nyitray, László, Reutzel, Robbie, Himmel, Daniel M., O'Neall-Hennessey, Elizabeth, Reshetnikova, Ludmilla, Szent-Györgyi, Andrew G., Brown, Jerry H., Cohen, Carolyn
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container_end_page 564
container_issue 5
container_start_page 553
container_title Structure (London)
container_volume 15
creator Yang, Yuting
Gourinath, S.
Kovács, Mihály
Nyitray, László
Reutzel, Robbie
Himmel, Daniel M.
O'Neall-Hennessey, Elizabeth
Reshetnikova, Ludmilla
Szent-Györgyi, Andrew G.
Brown, Jerry H.
Cohen, Carolyn
description 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.
doi_str_mv 10.1016/j.str.2007.03.010
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subjects Allosteric Regulation - physiology
Animals
CELLBIO
Crystallography, X-Ray
Decapodiformes - chemistry
Decapodiformes - metabolism
Myosins - chemistry
Myosins - physiology
Pectinidae - chemistry
Pectinidae - metabolism
Protein Conformation
Rigor Mortis - metabolism
Signal Transduction - physiology
title Rigor-like Structures from Muscle Myosins Reveal Key Mechanical Elements in the Transduction Pathways of This Allosteric Motor
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