8f8t: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8f8t]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F8T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F8T FirstGlance]. <br> | <table><tr><td colspan='2'>[[8f8t]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F8T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F8T 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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.26Å</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=8f8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f8t OCA], [https://pdbe.org/8f8t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f8t RCSB], [https://www.ebi.ac.uk/pdbsum/8f8t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f8t 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=8f8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f8t OCA], [https://pdbe.org/8f8t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f8t RCSB], [https://www.ebi.ac.uk/pdbsum/8f8t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f8t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 08:54, 5 July 2023
Cryo-EM structure of the Tropomodulin-capped pointed end of F-actinCryo-EM structure of the Tropomodulin-capped pointed end of F-actin
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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