View source for 5hmp


==Myosin Vc pre-powerstroke state==
<StructureSection load='5hmp' size='340' side='right'caption='[[5hmp]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hmp]] 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=5HMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HMP 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]] 2.397&#8491;</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=DMS:DIMETHYL+SULFOXIDE'>DMS</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=5hmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hmp OCA], [https://pdbe.org/5hmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hmp RCSB], [https://www.ebi.ac.uk/pdbsum/5hmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hmp 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 ==
Myosin X has features not found in other myosins. Its structure must underlie its unique ability to generate filopodia, which are essential for neuritogenesis, wound healing, cancer metastasis and some pathogenic infections. By determining high-resolution structures of key components of this motor, and characterizing the in vitro behaviour of the native dimer, we identify the features that explain the myosin X dimer behaviour. Single-molecule studies demonstrate that a native myosin X dimer moves on actin bundles with higher velocities and takes larger steps than on single actin filaments. The largest steps on actin bundles are larger than previously reported for artificially dimerized myosin X constructs or any other myosin. Our model and kinetic data explain why these large steps and high velocities can only occur on bundled filaments. Thus, myosin X functions as an antiparallel dimer in cells with a unique geometry optimized for movement on actin bundles.

The myosin X motor is optimized for movement on actin bundles.,Ropars V, Yang Z, Isabet T, Blanc F, Zhou K, Lin T, Liu X, Hissier P, Samazan F, Amigues B, Yang ED, Park H, Pylypenko O, Cecchini M, Sindelar CV, Sweeney HL, Houdusse A Nat Commun. 2016 Sep 1;7:12456. doi: 10.1038/ncomms12456. PMID:27580874<ref>PMID:27580874</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hmp" style="background-color:#fffaf0;"></div>

==See Also==
*[[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 HL]]