5i4e

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(New page: '''Unreleased structure''' The entry 5i4e is ON HOLD Authors: Chinthalapudi, K., Heissler, S.M., Preller, M., Sellers, J.R., Manstein, D.J. Description: Crystal Structure of Human Nonm...)
Current revision (08:22, 23 August 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 5i4e is ON HOLD
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==Crystal Structure of Human Nonmuscle Myosin 2C motor domain==
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<StructureSection load='5i4e' size='340' side='right'caption='[[5i4e]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5i4e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5I4E FirstGlance]. <br>
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</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AOV:ADP+ORTHOVANADATE'>AOV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5i4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i4e OCA], [https://pdbe.org/5i4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i4e RCSB], [https://www.ebi.ac.uk/pdbsum/5i4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i4e ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/MYH14_HUMAN MYH14_HUMAN] Peripheral neuropathy-myopathy-hoarseness-hearing loss syndrome;Autosomal dominant non-syndromic sensorineural deafness type DFNA. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/ACTNA_DICDI ACTNA_DICDI] F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Increases the actin-stimulated ATPase activity of myosin. Involved in vegetative cell growth, phagocytosis, motility and development, probably through stabilization of the actin network in the cortical cytoskeleton.<ref>PMID:10411959</ref> <ref>PMID:10413681</ref> <ref>PMID:10704840</ref> <ref>PMID:1732064</ref> <ref>PMID:3956480</ref> <ref>PMID:6746725</ref> <ref>PMID:8486739</ref> <ref>PMID:8937986</ref> [https://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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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Authors: Chinthalapudi, K., Heissler, S.M., Preller, M., Sellers, J.R., Manstein, D.J.
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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>
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Description: Crystal Structure of Human Nonmuscle Myosin 2C motor domain
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Heissler, S.M]]
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<div class="pdbe-citations 5i4e" style="background-color:#fffaf0;"></div>
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[[Category: Preller, M]]
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== References ==
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[[Category: Sellers, J.R]]
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<references/>
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[[Category: Chinthalapudi, K]]
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__TOC__
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[[Category: Manstein, D.J]]
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</StructureSection>
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[[Category: Dictyostelium discoideum]]
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Chinthalapudi K]]
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[[Category: Heissler SM]]
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[[Category: Manstein DJ]]
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[[Category: Preller M]]
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[[Category: Sellers JR]]

Current revision

Crystal Structure of Human Nonmuscle Myosin 2C motor domain

PDB ID 5i4e

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