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5yu8

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'''Unreleased structure'''
 
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The entry 5yu8 is ON HOLD until Paper Publication
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==Cofilin decorated actin filament==
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<StructureSection load='5yu8' size='340' side='right' caption='[[5yu8]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5yu8]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YU8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YU8 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>
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<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=5yu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yu8 OCA], [http://pdbe.org/5yu8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yu8 RCSB], [http://www.ebi.ac.uk/pdbsum/5yu8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yu8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://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. [[http://www.uniprot.org/uniprot/COF2_CHICK COF2_CHICK]] Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Actin depolymerizing factor (ADF) and cofilin accelerate actin dynamics by severing and disassembling actin filaments. Here, we present the 3.8 A resolution cryo-EM structure of cofilactin (cofilin-decorated actin filament). The actin subunit structure of cofilactin (C-form) is distinct from those of F-actin (F-form) and monomeric actin (G-form). During the transition between these three conformations, the inner domain of actin (subdomains 3 and 4) and the majority of subdomain 1 move as two separate rigid bodies. The cofilin-actin interface consists of three distinct parts. Based on the rigid body movements of actin and the three cofilin-actin interfaces, we propose models for the cooperative binding of cofilin to actin, preferential binding of cofilin to ADP-bound actin filaments and cofilin-mediated severing of actin filaments.
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Authors:
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Structural basis for cofilin binding and actin filament disassembly.,Tanaka K, Takeda S, Mitsuoka K, Oda T, Kimura-Sakiyama C, Maeda Y, Narita A Nat Commun. 2018 May 10;9(1):1860. doi: 10.1038/s41467-018-04290-w. PMID:29749375<ref>PMID:29749375</ref>
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Description:
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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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<div class="pdbe-citations 5yu8" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Narita, A]]
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[[Category: Tanaka, K]]
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[[Category: Actin]]
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[[Category: Cofilin]]
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[[Category: Cytoskeleton]]
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[[Category: Cytosolic protein]]
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[[Category: Muscle]]

Revision as of 07:18, 23 May 2018

Cofilin decorated actin filament

5yu8, resolution 3.80Å

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