2os8
From Proteopedia
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|PDB= 2os8 |SIZE=350|CAPTION= <scene name='initialview01'>2os8</scene>, resolution 3.270Å | |PDB= 2os8 |SIZE=350|CAPTION= <scene name='initialview01'>2os8</scene>, resolution 3.270Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1kk7|1KK7]], [[1kk8|1KK8]], [[1sr6|1SR6]], [[1oe9|1OE9]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2os8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2os8 OCA], [http://www.ebi.ac.uk/pdbsum/2os8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2os8 RCSB]</span> | ||
}} | }} | ||
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[[Category: Gourinath, S.]] | [[Category: Gourinath, S.]] | ||
[[Category: Yang, Y.]] | [[Category: Yang, Y.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: MG]] | ||
[[Category: mechanical element]] | [[Category: mechanical element]] | ||
[[Category: motor]] | [[Category: motor]] | ||
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[[Category: rigor-like]] | [[Category: rigor-like]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:22:24 2008'' |
Revision as of 01:22, 31 March 2008
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| , resolution 3.270Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1KK7, 1KK8, 1SR6, 1OE9
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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