4e7s: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4e7s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E7S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E7S FirstGlance]. <br>
-</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</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=4e7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e7s OCA], [https://pdbe.org/4e7s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e7s RCSB], [https://www.ebi.ac.uk/pdbsum/4e7s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e7s ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/F1RQI7_PIG F1RQI7_PIG]]
+[https://www.uniprot.org/uniprot/F1RQI7_PIG F1RQI7_PIG]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Myosin VI is the only known reverse-direction myosin motor. It has an unprecedented means of amplifying movements within the motor involving rearrangements of the converter subdomain at the C terminus of the motor and an unusual lever arm projecting from the converter. While the average step size of a myosin VI dimer is 30-36 nm, the step size is highly variable, presenting a challenge to the lever arm mechanism by which all myosins are thought to move. Herein, we present structures of myosin VI that reveal regions of compliance that allow an uncoupling of the lead head when movement is modeled on actin. The location of the compliance restricts the possible actin binding sites and predicts the observed stepping behavior. The model reveals that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model.
-Processive Steps in the Reverse Direction Require Uncoupling of the Lead Head Lever Arm of Myosin VI.,Menetrey J, Isabet T, Ropars V, Mukherjea M, Pylypenko O, Liu X, Perez J, Vachette P, Sweeney HL, Houdusse AM Mol Cell. 2012 Aug 29. PMID:22940248<ref>PMID:22940248</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4e7s" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Myosin 3D Structures|Myosin 3D Structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>