5h53
From Proteopedia
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(New page: '''Unreleased structure''' The entry 5h53 is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The structure of rabbit skeletal muscle actomyosin rigor complex at 5.2 angstrom.== |
| + | <SX load='5h53' size='340' side='right' viewer='molstar' caption='[[5h53]], [[Resolution|resolution]] 5.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5h53]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H53 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5.2Å</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=HIC:4-METHYL-HISTIDINE'>HIC</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=5h53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h53 OCA], [https://pdbe.org/5h53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h53 RCSB], [https://www.ebi.ac.uk/pdbsum/5h53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h53 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9GJP9_RABIT Q9GJP9_RABIT] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Muscle contraction is driven by cyclic association and dissociation of myosin head of the thick filament with thin actin filament coupled with ATP binding and hydrolysis by myosin. However, because of the absence of actomyosin rigour structure at high resolution, it still remains unclear how the strong binding of myosin to actin filament triggers the release of hydrolysis products and how ATP binding causes their dissociation. Here we report the structure of mammalian skeletal muscle actomyosin rigour complex at 5.2 A resolution by electron cryomicroscopy. Comparison with the structures of myosin in various states shows a distinctly large conformational change, providing insights into the ATPase-coupled reaction cycle of actomyosin. Based on our observations, we hypothesize that asymmetric binding along the actin filament could function as a Brownian ratchet by favouring directionally biased thermal motions of myosin and actin. | ||
| - | + | Structure of actomyosin rigour complex at 5.2 A resolution and insights into the ATPase cycle mechanism.,Fujii T, Namba K Nat Commun. 2017 Jan 9;8:13969. doi: 10.1038/ncomms13969. PMID:28067235<ref>PMID:28067235</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5h53" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Actin 3D structures|Actin 3D structures]] | ||
| + | *[[Myosin 3D Structures|Myosin 3D Structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Oryctolagus cuniculus]] | ||
| + | [[Category: Fujii T]] | ||
| + | [[Category: Namba K]] | ||
Current revision
The structure of rabbit skeletal muscle actomyosin rigor complex at 5.2 angstrom.
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