8f8s: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 8f8s is ON HOLD
+==Cryo-EM structure of the free pointed end of F-actin==
+<StructureSection load='8f8s' size='340' side='right'caption='[[8f8s]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8f8s]] 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=8F8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F8S FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.84&#8491;</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=8f8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f8s OCA], [https://pdbe.org/8f8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f8s RCSB], [https://www.ebi.ac.uk/pdbsum/8f8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f8s 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 8f8s" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Oryctolagus cuniculus]]
+[[Category: Barrie KR]]
+[[Category: Carman PJ]]
+[[Category: Dominguez R]]