Summary for 3I5G
| Entry DOI | 10.2210/pdb3i5g/pdb |
| Related | 2OY6 3I5F 3I5H 3I5I |
| Descriptor | Myosin heavy chain isoform A, Myosin regulatory light chain LC-2, mantle muscle, Myosin catalytic light chain LC-1, mantle muscle, ... (6 entities in total) |
| Functional Keywords | rigor-like, squid, muscle myosin, contractile protein |
| Biological source | Loligo pealei (longfin inshore squid) More |
| Total number of polymer chains | 3 |
| Total formula weight | 131740.47 |
| Authors | Yang, Y.,Gourinath, S.,Kovacs, M.,Nyitray, L.,Reutzel, R.,Himmel, D.M.,O'Neall-Hennessey, E.,Reshetnikova, L.,Szent-Gyorgyi, A.G.,Brown, J.H.,Cohen, C. (deposition date: 2009-07-05, release date: 2009-07-28, Last modification date: 2023-09-06) |
| Primary citation | Yang, Y.,Gourinath, S.,Kovacs, M.,Nyitray, L.,Reutzel, R.,Himmel, D.M.,O'Neall-Hennessey, E.,Reshetnikova, L.,Szent-Gyorgyi, A.G.,Brown, J.H.,Cohen, C. Rigor-like structures from muscle myosins reveal key mechanical elements in the transduction pathways of this allosteric motor. Structure, 15:553-564, 2007 Cited by PubMed Abstract: 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. PubMed: 17502101DOI: 10.1016/j.str.2007.03.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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