5i4e
From Proteopedia
(Difference between revisions)
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==Crystal Structure of Human Nonmuscle Myosin 2C motor domain== | ==Crystal Structure of Human Nonmuscle Myosin 2C motor domain== | ||
| - | <StructureSection load='5i4e' size='340' side='right' caption='[[5i4e]], [[Resolution|resolution]] 2.25Å' scene=''> | + | <StructureSection load='5i4e' size='340' side='right'caption='[[5i4e]], [[Resolution|resolution]] 2.25Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5i4e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I4E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5i4e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I4E FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AOV:ADP+ORTHOVANADATE'>AOV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AOV:ADP+ORTHOVANADATE'>AOV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">abpA, actnA, DDB_G0268632 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5i4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i4e OCA], [http://pdbe.org/5i4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i4e RCSB], [http://www.ebi.ac.uk/pdbsum/5i4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i4e ProSAT]</span></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=5i4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i4e OCA], [http://pdbe.org/5i4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i4e RCSB], [http://www.ebi.ac.uk/pdbsum/5i4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i4e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/MYH14_HUMAN MYH14_HUMAN]] Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. | [[http://www.uniprot.org/uniprot/MYH14_HUMAN MYH14_HUMAN]] Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Despite a generic, highly conserved motor domain, ATP turnover kinetics and their activation by F-actin vary greatly between myosin-2 isoforms. Here, we present a 2.25 A pre-powerstroke state (ADPVO4) crystal structure of the human nonmuscle myosin-2C motor domain, one of the slowest myosins characterized. In combination with integrated mutagenesis, ensemble-solution kinetics, and molecular dynamics simulation approaches, the structure reveals an allosteric communication pathway that connects the distal end of the motor domain with the active site. Disruption of this pathway by mutation of hub residue R788, which forms the center of a cluster of interactions connecting the converter, the SH1-SH2 helix, the relay helix, and the lever, abolishes nonmuscle myosin-2 specific kinetic signatures. Our results provide insights into structural changes in the myosin motor domain that are triggered upon F-actin binding and contribute critically to the mechanochemical behavior of stress fibers, actin arcs, and cortical actin-based structures. | ||
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| + | Mechanistic insights into the active site and allosteric communication pathways in human nonmuscle myosin-2C.,Chinthalapudi K, Heissler SM, Preller M, Sellers JR, Manstein DJ Elife. 2017 Dec 19;6. pii: 32742. doi: 10.7554/eLife.32742. PMID:29256864<ref>PMID:29256864</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5i4e" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Chinthalapudi, K]] | [[Category: Chinthalapudi, K]] | ||
[[Category: Heissler, S M]] | [[Category: Heissler, S M]] | ||
Revision as of 06:53, 27 March 2019
Crystal Structure of Human Nonmuscle Myosin 2C motor domain
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