6bnp
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==CryoEM structure of MyosinVI-actin complex in the rigor (nucleotide-free) state== | |
| + | <StructureSection load='6bnp' size='340' side='right' caption='[[6bnp]], [[Resolution|resolution]] 4.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6bnp]] 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=6BNP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BNP 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=MG:MAGNESIUM+ION'>MG</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=6bnp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bnp OCA], [http://pdbe.org/6bnp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bnp RCSB], [http://www.ebi.ac.uk/pdbsum/6bnp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bnp 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: Gurel, P | + | <div class="pdbe-citations 6bnp" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Oryctolagus cuniculus]] | ||
| + | [[Category: Alushin, G A]] | ||
| + | [[Category: Gurel, P S]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Contractile protein]] | ||
| + | [[Category: Cytoskeleton]] | ||
| + | [[Category: Filament]] | ||
Revision as of 08:32, 10 January 2018
CryoEM structure of MyosinVI-actin complex in the rigor (nucleotide-free) state
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