7rb8: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==== | ==cryo-EM structure of the ADP state wild type myosin-15-F-actin complex== | ||
<StructureSection load='7rb8' size='340' side='right'caption='[[7rb8]]' scene=''> | <StructureSection load='7rb8' size='340' side='right'caption='[[7rb8]], [[Resolution|resolution]] 3.63Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7rb8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RB8 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=7rb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rb8 OCA], [https://pdbe.org/7rb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rb8 RCSB], [https://www.ebi.ac.uk/pdbsum/7rb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rb8 ProSAT]</span></td></tr> | </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=HIC:4-METHYL-HISTIDINE'>HIC</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=7rb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rb8 OCA], [https://pdbe.org/7rb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rb8 RCSB], [https://www.ebi.ac.uk/pdbsum/7rb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rb8 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/ACTS_CHICK ACTS_CHICK]] 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 == | |||
The motor protein myosin-15 is necessary for the development and maintenance of mechanosensory stereocilia, and mutations in myosin-15 cause hereditary deafness. In addition to transporting actin regulatory machinery to stereocilia tips, myosin-15 directly nucleates actin filament ("F-actin") assembly, which is disrupted by a progressive hearing loss mutation (p.D1647G, "jordan"). Here, we present cryo-electron microscopy structures of myosin-15 bound to F-actin, providing a framework for interpreting the impacts of deafness mutations on motor activity and actin nucleation. Rigor myosin-15 evokes conformational changes in F-actin yet maintains flexibility in actin's D-loop, which mediates inter-subunit contacts, while the jordan mutant locks the D-loop in a single conformation. Adenosine diphosphate-bound myosin-15 also locks the D-loop, which correspondingly blunts actin-polymerization stimulation. We propose myosin-15 enhances polymerization by bridging actin protomers, regulating nucleation efficiency by modulating actin's structural plasticity in a myosin nucleotide state-dependent manner. This tunable regulation of actin polymerization could be harnessed to precisely control stereocilium height. | |||
Structural basis for tunable control of actin dynamics by myosin-15 in mechanosensory stereocilia.,Gong R, Jiang F, Moreland ZG, Reynolds MJ, de Los Reyes SE, Gurel P, Shams A, Heidings JB, Bowl MR, Bird JE, Alushin GM Sci Adv. 2022 Jul 22;8(29):eabl4733. doi: 10.1126/sciadv.abl4733. Epub 2022 Jul, 20. PMID:35857845<ref>PMID:35857845</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7rb8" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Actin 3D structures|Actin 3D structures]] | |||
*[[Myosin 3D Structures|Myosin 3D Structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Gallus gallus]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Alushin GM]] | |||
[[Category: Gong R]] | |||
[[Category: Gurel P]] | |||
[[Category: Reynolds MJ]] | |||
Latest revision as of 06:51, 8 September 2022
cryo-EM structure of the ADP state wild type myosin-15-F-actin complexcryo-EM structure of the ADP state wild type myosin-15-F-actin complex
Structural highlights
Function[ACTS_CHICK] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Publication Abstract from PubMedThe motor protein myosin-15 is necessary for the development and maintenance of mechanosensory stereocilia, and mutations in myosin-15 cause hereditary deafness. In addition to transporting actin regulatory machinery to stereocilia tips, myosin-15 directly nucleates actin filament ("F-actin") assembly, which is disrupted by a progressive hearing loss mutation (p.D1647G, "jordan"). Here, we present cryo-electron microscopy structures of myosin-15 bound to F-actin, providing a framework for interpreting the impacts of deafness mutations on motor activity and actin nucleation. Rigor myosin-15 evokes conformational changes in F-actin yet maintains flexibility in actin's D-loop, which mediates inter-subunit contacts, while the jordan mutant locks the D-loop in a single conformation. Adenosine diphosphate-bound myosin-15 also locks the D-loop, which correspondingly blunts actin-polymerization stimulation. We propose myosin-15 enhances polymerization by bridging actin protomers, regulating nucleation efficiency by modulating actin's structural plasticity in a myosin nucleotide state-dependent manner. This tunable regulation of actin polymerization could be harnessed to precisely control stereocilium height. Structural basis for tunable control of actin dynamics by myosin-15 in mechanosensory stereocilia.,Gong R, Jiang F, Moreland ZG, Reynolds MJ, de Los Reyes SE, Gurel P, Shams A, Heidings JB, Bowl MR, Bird JE, Alushin GM Sci Adv. 2022 Jul 22;8(29):eabl4733. doi: 10.1126/sciadv.abl4733. Epub 2022 Jul, 20. PMID:35857845[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||