8f8r
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the free barbed end of F-actin== | |
| + | <StructureSection load='8f8r' size='340' side='right'caption='[[8f8r]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8f8r]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F8R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F8R FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=8f8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f8r OCA], [https://pdbe.org/8f8r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f8r RCSB], [https://www.ebi.ac.uk/pdbsum/8f8r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f8r ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT] 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 == | ||
| + | The barbed and pointed ends of the actin filament (F-actin) are the sites of growth/shrinkage and the targets of capping proteins that block subunit exchange, including CapZ at the barbed end and tropomodulin at the pointed end. We describe cryo-electron microscopy structures of the free and capped ends of F-actin. Terminal subunits at the free barbed end adopt a "flat" F-actin conformation. CapZ binds with minor changes to the barbed end but major changes to itself. In contrast, subunits at the free pointed end adopt a "twisted" G-actin conformation. Tropomodulin binding forces the second subunit into an F-actin conformation. The structures reveal how the ends differ from the middle in F-actin and how these differences control subunit addition/dissociation, capping, and interactions with end-binding proteins. | ||
| - | + | Structures of the free and capped ends of the actin filament.,Carman PJ, Barrie KR, Rebowski G, Dominguez R Science. 2023 May 25:eadg6812. doi: 10.1126/science.adg6812. PMID:37228182<ref>PMID:37228182</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8f8r" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Oryctolagus cuniculus]] | ||
| + | [[Category: Barrie KR]] | ||
| + | [[Category: Carman PJ]] | ||
| + | [[Category: Dominguez R]] | ||
Revision as of 05:40, 7 June 2023
Cryo-EM structure of the free barbed end of F-actin
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