4zg4
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Myosin Vc Pre-powerstroke== | |
| + | <StructureSection load='4zg4' size='340' side='right' caption='[[4zg4]], [[Resolution|resolution]] 2.36Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4zg4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZG4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZG4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zg4 OCA], [http://pdbe.org/4zg4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zg4 RCSB], [http://www.ebi.ac.uk/pdbsum/4zg4 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MYO5C_HUMAN MYO5C_HUMAN]] May be involved in transferrin trafficking. Likely to power actin-based membrane trafficking in many physiologically crucial tissues. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Molecular motors produce force when they interact with their cellular tracks. For myosin motors, the primary force-generating state has MgADP tightly bound, whereas myosin is strongly bound to actin. We have generated an 8-A cryoEM reconstruction of this state for myosin V and used molecular dynamics flexed fitting for model building. We compare this state to the subsequent state on actin (Rigor). The ADP-bound structure reveals that the actin-binding cleft is closed, even though MgADP is tightly bound. This state is accomplished by a previously unseen conformation of the beta-sheet underlying the nucleotide pocket. The transition from the force-generating ADP state to Rigor requires a 9.5 degrees rotation of the myosin lever arm, coupled to a beta-sheet rearrangement. Thus, the structure reveals the detailed rearrangements underlying myosin force generation as well as the basis of strain-dependent ADP release that is essential for processive myosins, such as myosin V. | ||
| - | + | Force-producing ADP state of myosin bound to actin.,Wulf SF, Ropars V, Fujita-Becker S, Oster M, Hofhaus G, Trabuco LG, Pylypenko O, Sweeney HL, Houdusse AM, Schroder RR Proc Natl Acad Sci U S A. 2016 Mar 29;113(13):E1844-52. doi:, 10.1073/pnas.1516598113. Epub 2016 Mar 14. PMID:26976594<ref>PMID:26976594</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 4zg4" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Houdusse, A]] | [[Category: Houdusse, A]] | ||
| - | [[Category: | + | [[Category: Pylypenko, O]] |
[[Category: Ropars, V]] | [[Category: Ropars, V]] | ||
| + | [[Category: Sweeney, L]] | ||
| + | [[Category: Motor protein]] | ||
| + | [[Category: Myosin]] | ||
| + | [[Category: Pre-powerstroke]] | ||
Revision as of 18:11, 10 May 2016
Myosin Vc Pre-powerstroke
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