4zg4: Difference between revisions
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==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 with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4ZG4 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]] 2.36Å</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=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'>[https://proteopedia.org/fgij/fg.htm?mol=4zg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zg4 OCA], [https://pdbe.org/4zg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zg4 RCSB], [https://www.ebi.ac.uk/pdbsum/4zg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zg4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://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> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4zg4" style="background-color:#fffaf0;"></div> | ||
[[Category: Pylypenko | |||
[[Category: | ==See Also== | ||
[[Category: Sweeney | *[[Myosin 3D Structures|Myosin 3D Structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Houdusse A]] | |||
[[Category: Pylypenko O]] | |||
[[Category: Ropars V]] | |||
[[Category: Sweeney L]] | |||
