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| | ==Structure of bare actin filament, backbone-averaged with sidechains truncated to alanine== | | ==Structure of bare actin filament, backbone-averaged with sidechains truncated to alanine== |
| - | <StructureSection load='6bnu' size='340' side='right' caption='[[6bnu]], [[Resolution|resolution]] 7.50Å' scene=''> | + | <SX load='6bnu' size='340' side='right' viewer='molstar' caption='[[6bnu]], [[Resolution|resolution]] 7.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6bnu]] 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=6BNU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BNU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6bnu]] 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=6BNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BNU FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6bno|6bno]]</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]] 7.5Å</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=6bnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bnu OCA], [http://pdbe.org/6bnu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bnu RCSB], [http://www.ebi.ac.uk/pdbsum/6bnu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bnu ProSAT]</span></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=6bnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bnu OCA], [https://pdbe.org/6bnu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bnu RCSB], [https://www.ebi.ac.uk/pdbsum/6bnu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bnu 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;">
| + | |
| - | == 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.
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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>
| + | |
| - | <div class="pdbe-citations 6bnu" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
| + | |
| | __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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