Source:http://linkedlifedata.com/resource/pubmed/id/20946985
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rdf:type | |
lifeskim:mentions |
umls-concept:C0001271,
umls-concept:C0030685,
umls-concept:C0031603,
umls-concept:C0205421,
umls-concept:C0391871,
umls-concept:C0678594,
umls-concept:C0680255,
umls-concept:C1283071,
umls-concept:C1510699,
umls-concept:C1527178,
umls-concept:C1706853,
umls-concept:C1879547,
umls-concept:C1879748,
umls-concept:C1963578
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pubmed:issue |
2
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pubmed:dateCreated |
2010-10-15
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pubmed:databankReference | |
pubmed:abstractText |
Assembled actin filaments support cellular signaling, intracellular trafficking, and cytokinesis. ATP hydrolysis triggered by actin assembly provides the structural cues for filament turnover in vivo. Here, we present the cryo-electron microscopic (cryo-EM) structure of filamentous actin (F-actin) in the presence of phosphate, with the visualization of some ?-helical backbones and large side chains. A complete atomic model based on the EM map identified intermolecular interactions mediated by bound magnesium and phosphate ions. Comparison of the F-actin model with G-actin monomer crystal structures reveals a critical role for bending of the conserved proline-rich loop in triggering phosphate release following ATP hydrolysis. Crystal structures of G-actin show that mutations in this loop trap the catalytic site in two intermediate states of the ATPase cycle. The combined structural information allows us to propose a detailed molecular mechanism for the biochemical events, including actin polymerization and ATPase activation, critical for actin filament dynamics.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1097-4172
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2010 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
143
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
275-87
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pubmed:meshHeading |
pubmed-meshheading:20946985-Actins,
pubmed-meshheading:20946985-Adenosine Triphosphate,
pubmed-meshheading:20946985-Animals,
pubmed-meshheading:20946985-Cryoelectron Microscopy,
pubmed-meshheading:20946985-Crystallography, X-Ray,
pubmed-meshheading:20946985-Models, Molecular,
pubmed-meshheading:20946985-Muscle, Skeletal,
pubmed-meshheading:20946985-Phosphates,
pubmed-meshheading:20946985-Rabbits
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pubmed:year |
2010
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pubmed:articleTitle |
Structural basis for actin assembly, activation of ATP hydrolysis, and delayed phosphate release.
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pubmed:affiliation |
Department of Biosciences, School of Science and Engineering, Teikyo University, Toyosatodai 1-1, Utsunomiya 320-8551, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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