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== | ==Rigor-like structures of muscle myosins reveal key mechanical elements in the transduction pathways of this allosteric motor== | ||
<StructureSection load='2otg' size='340' side='right'caption='[[2otg]], [[Resolution|resolution]] 3.12Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2otg]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Placopecten_magellanicus Placopecten magellanicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OTG FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.12Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2otg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2otg OCA], [https://pdbe.org/2otg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2otg RCSB], [https://www.ebi.ac.uk/pdbsum/2otg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2otg ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q26080_PLAMG Q26080_PLAMG] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ot/2otg_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2otg ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | 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. | ||
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<ref>PMID:17502101</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2otg" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Myosin 3D Structures|Myosin 3D Structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Placopecten magellanicus]] | [[Category: Placopecten magellanicus]] | ||
[[Category: Brown JH]] | |||
[[Category: Brown | [[Category: Cohen C]] | ||
[[Category: Cohen | [[Category: Gourinath S]] | ||
[[Category: Gourinath | [[Category: Himmel DM]] | ||
[[Category: Himmel | [[Category: Kovacs M]] | ||
[[Category: Kovacs | [[Category: Nyitray L]] | ||
[[Category: | [[Category: O'Neall-Hennessey E]] | ||
[[Category: | [[Category: Reshetnikova L]] | ||
[[Category: Reshetnikova | [[Category: Reutzel R]] | ||
[[Category: Reutzel | [[Category: Szent-Gyorgyi AG]] | ||
[[Category: Szent-Gyorgyi | [[Category: Yang Y]] | ||
[[Category: Yang | |||
Latest revision as of 13:48, 30 August 2023
Rigor-like structures of muscle myosins reveal key mechanical elements in the transduction pathways of this allosteric motorRigor-like structures of muscle myosins reveal key mechanical elements in the transduction pathways of this allosteric motor
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedUnlike 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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