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3j0s

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Remodeling of actin filaments by ADF cofilin proteins

3j0s, resolution 9.00Å

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 ==Remodeling of actin filaments by ADF cofilin proteins==
-<StructureSection load='3j0s' size='340' side='right' caption='[[3j0s]], [[Resolution|resolution]] 9.00&Aring;' scene=''>
+<SX load='3j0s' size='340' side='right' viewer='molstar' caption='[[3j0s]], [[Resolution|resolution]] 9.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3j0s]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J0S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J0S FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3j0s]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] 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=3J0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J0S FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CFL1, CFL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 9&#8491;</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=3j0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j0s OCA], [http://pdbe.org/3j0s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j0s RCSB], [http://www.ebi.ac.uk/pdbsum/3j0s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j0s ProSAT]</span></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=3j0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j0s OCA], [https://pdbe.org/3j0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j0s RCSB], [https://www.ebi.ac.uk/pdbsum/3j0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j0s ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ACTB_CHICK ACTB_CHICK]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
+[https://www.uniprot.org/uniprot/ACTB_CHICK ACTB_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 ==
-Cofilin/ADF proteins play key roles in the dynamics of actin, one of the most abundant and highly conserved eukaryotic proteins. We used cryoelectron microscopy to generate a 9-A resolution three-dimensional reconstruction of cofilin-decorated actin filaments, the highest resolution achieved for a complex of F-actin with an actin-binding protein. We show that the cofilin-induced change in the filament twist is due to a unique conformation of the actin molecule unrelated to any previously observed state. The changes between the actin protomer in naked F-actin and in the actin-cofilin filament are greater than the conformational changes between G- and F-actin. Our results show the structural plasticity of actin, suggest that other actin-binding proteins may also induce large but different conformational changes, and show that F-actin cannot be described by a single molecular model.
-Remodeling of actin filaments by ADF/cofilin proteins.,Galkin VE, Orlova A, Kudryashov DS, Solodukhin A, Reisler E, Schroder GF, Egelman EH Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20568-72. Epub 2011 Dec 7. PMID:22158895<ref>PMID:22158895</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3j0s" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Actin|Actin]]
+*[[Actin 3D structures|Actin 3D structures]]
-== References ==
-<references/>
 __TOC__
-</StructureSection>
+</SX>
 [[Category: Gallus gallus]]
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Egelman, E H]]
+[[Category: Large Structures]]
-[[Category: Galkin, V E]]
+[[Category: Egelman EH]]
-[[Category: Kudryashov, D S]]
+[[Category: Galkin VE]]
-[[Category: Orlova, A]]
+[[Category: Kudryashov DS]]
-[[Category: Reisler, E]]
+[[Category: Orlova A]]
-[[Category: Schroeder, G F]]
+[[Category: Reisler E]]
-[[Category: Solodukhin, A]]
+[[Category: Schroeder GF]]
-[[Category: Contractile protein-actin binding protein complex]]
+[[Category: Solodukhin A]]
-[[Category: Contractile protein-protein binding complex]]
-[[Category: Helical polymer]]

3j0s

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Remodeling of actin filaments by ADF cofilin proteins

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