6bno: Difference between revisions

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-'''Unreleased structure'''
-The entry 6bno is ON HOLD
+==Structure of bare actin filament==
+<StructureSection load='6bno' size='340' side='right' caption='[[6bno]], [[Resolution|resolution]] 5.50&Aring;' scene=''>
+== 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>
+</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=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>
+</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.
-Authors: Gurel, P.S., Alushin, G.A.
+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>
-Description: Structure of bare actin filament
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Gurel, P.S]]
+<div class="pdbe-citations 6bno" style="background-color:#fffaf0;"></div>
-[[Category: Alushin, G.A]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Oryctolagus cuniculus]]
+[[Category: Alushin, G A]]
+[[Category: Gurel, P S]]
+[[Category: Contractile protein]]
+[[Category: Cytoskeleton]]
+[[Category: Filament]]