2os8

From Proteopedia

Revision as of 16:03, 20 March 2008

Rigor-like structures of muscle myosins reveal key mechanical elements in the transduction pathways of this allosteric motor

Overview

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.

About this Structure

2OS8 is a Protein complex structure of sequences from Placopecten magellanicus. Full crystallographic information is available from OCA.

Reference

Rigor-like structures from muscle myosins reveal key mechanical elements in the transduction pathways of this allosteric motor., Yang Y, Gourinath S, Kovacs M, Nyitray L, Reutzel R, Himmel DM, O'Neall-Hennessey E, Reshetnikova L, Szent-Gyorgyi AG, Brown JH, Cohen C, Structure. 2007 May;15(5):553-64. PMID:17502101

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