7yv9
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of full-length Myosin Va in the autoinhibited state== | |
| + | <StructureSection load='7yv9' size='340' side='right'caption='[[7yv9]], [[Resolution|resolution]] 4.78Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7yv9]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YV9 FirstGlance]. <br> | ||
| + | </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=7yv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yv9 OCA], [https://pdbe.org/7yv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yv9 RCSB], [https://www.ebi.ac.uk/pdbsum/7yv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yv9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/D3YZ62_MOUSE D3YZ62_MOUSE] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | As the prototype of unconventional myosin motor family, myosin Va (MyoVa) transport cellular cargos along actin filaments in diverse cellular processes. The off-duty MyoVa adopts a closed and autoinhibited state, which can be relieved by cargo binding. The molecular mechanisms governing the autoinhibition and activation of MyoVa remain unclear. Here, we report the cryo-electron microscopy structure of the two full-length, closed MyoVa heavy chains in complex with 12 calmodulin light chains at 4.78-A resolution. The MyoVa adopts a triangular structure with multiple intra- and interpolypeptide chain interactions in establishing the closed state with cargo binding and adenosine triphosphatase activity inhibited. Structural, biochemical, and cellular analyses uncover an asymmetric autoinhibition mechanism, in which the cargo-binding sites in the two MyoVa heavy chains are differently protected. Thus, specific and efficient MyoVa activation requires coincident binding of multiple cargo adaptors, revealing an intricate and elegant activity regulation of the motor in response to cargos. | ||
| - | + | Autoinhibition and activation mechanisms revealed by the triangular-shaped structure of myosin Va.,Niu F, Liu Y, Sun K, Xu S, Dong J, Yu C, Yan K, Wei Z Sci Adv. 2022 Dec 9;8(49):eadd4187. doi: 10.1126/sciadv.add4187. Epub 2022 Dec 9. PMID:36490350<ref>PMID:36490350</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7yv9" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Niu F]] | ||
| + | [[Category: Wei Z]] | ||
Revision as of 09:26, 21 December 2022
Cryo-EM structure of full-length Myosin Va in the autoinhibited state
| |||||||||||
