6bnw: Difference between revisions
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==CryoEM structure of Myosin VI-Actin complex in the ADP state, backbone-averaged with side chains truncated to alanine== | |||
<StructureSection load='6bnw' size='340' side='right' caption='[[6bnw]], [[Resolution|resolution]] 5.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6bnw]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BNW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BNW FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6bnq|6bnq]]</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=6bnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bnw OCA], [http://pdbe.org/6bnw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bnw RCSB], [http://www.ebi.ac.uk/pdbsum/6bnw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bnw ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Despite extensive scrutiny of the myosin superfamily, the lack of high-resolution structures of actin-bound states has prevented a complete description of its mechanochemical cycle and limited insight into how sequence and structural diversification of the motor domain gives rise to specialized functional properties. Here we present cryo-EM structures of the unique minus-end directed myosin VI motor domain in rigor (4.6 A) and Mg-ADP (5.5 A) states bound to F-actin. Comparison to the myosin IIC-F-actin rigor complex reveals an almost complete lack of conservation of residues at the actin-myosin interface despite preservation of the primary sequence regions composing it, suggesting an evolutionary path for motor specialization. Additionally, analysis of the transition from ADP to rigor provides a structural rationale for force sensitivity in this step of the mechanochemical cycle. Finally, we observe reciprocal rearrangements in actin and myosin accompanying the transition between these states, supporting a role for actin structural plasticity during force generation by myosin VI. | |||
Cryo-EM structures reveal specialization at the myosin VI-actin interface and a mechanism of force sensitivity.,Gurel PS, Kim LY, Ruijgrok PV, Omabegho T, Bryant Z, Alushin GM Elife. 2017 Dec 4;6. doi: 10.7554/eLife.31125. PMID:29199952<ref>PMID:29199952</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Alushin, G | <div class="pdbe-citations 6bnw" style="background-color:#fffaf0;"></div> | ||
[[Category: Gurel, P | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Oryctolagus cuniculus]] | |||
[[Category: Alushin, G M]] | |||
[[Category: Gurel, P G]] | |||
[[Category: Complex]] | |||
[[Category: Contractile protein]] | |||
[[Category: Cytoskeleton]] | |||
[[Category: Filament]] | |||
