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| ==Structure of bare actin filament== | | ==Structure of bare actin filament== |
| <StructureSection load='6bno' size='340' side='right' caption='[[6bno]], [[Resolution|resolution]] 5.50Å' scene=''> | | <SX load='6bno' size='340' side='right' viewer='molstar' caption='[[6bno]], [[Resolution|resolution]] 5.50Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6bno]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BNO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BNO FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6bno]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BNO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BNO 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> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5.5Å</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=6bno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bno OCA], [http://pdbe.org/6bno PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bno RCSB], [http://www.ebi.ac.uk/pdbsum/6bno PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bno ProSAT]</span></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=MG:MAGNESIUM+ION'>MG</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=6bno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bno OCA], [https://pdbe.org/6bno PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bno RCSB], [https://www.ebi.ac.uk/pdbsum/6bno PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bno ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == 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. | | [https://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;">
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| == Publication Abstract from PubMed ==
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| 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.
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| 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>
| | ==See Also== |
| | | *[[Actin 3D structures|Actin 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6bno" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </SX> |
| | [[Category: Large Structures]] |
| [[Category: Oryctolagus cuniculus]] | | [[Category: Oryctolagus cuniculus]] |
| [[Category: Alushin, G A]] | | [[Category: Alushin GA]] |
| [[Category: Gurel, P S]] | | [[Category: Gurel PS]] |
| [[Category: Contractile protein]]
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| [[Category: Cytoskeleton]]
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| [[Category: Filament]]
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