8f8p: Difference between revisions
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==Cryo-EM structure of F-actin in the ADP state== | |||
<StructureSection load='8f8p' size='340' side='right'caption='[[8f8p]], [[Resolution|resolution]] 2.26Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8f8p]] is a 5 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=8F8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F8P 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]] 2.26Å</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=8f8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f8p OCA], [https://pdbe.org/8f8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f8p RCSB], [https://www.ebi.ac.uk/pdbsum/8f8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f8p 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 8f8p" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Oryctolagus cuniculus]] | |||
[[Category: Barrie KR]] | |||
[[Category: Carman PJ]] | |||
[[Category: Dominguez R]] | |||
Latest revision as of 08:54, 5 July 2023
Cryo-EM structure of F-actin in the ADP stateCryo-EM structure of F-actin in the ADP state
Structural highlights
FunctionACTS_RABIT Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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