5ly3
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==P. calidifontis crenactin in complex with arcadin-2 C-terminal peptide== | |
| + | <StructureSection load='5ly3' size='340' side='right' caption='[[5ly3]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ly3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LY3 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></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=5ly3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ly3 OCA], [http://pdbe.org/5ly3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ly3 RCSB], [http://www.ebi.ac.uk/pdbsum/5ly3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ly3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The similarity of eukaryotic actin to crenactin, a filament-forming protein from the crenarchaeon Pyrobaculum calidifontis supports the theory of a common origin of Crenarchaea and Eukaryotes. Monomeric structures of crenactin and actin are similar, although their filament architectures were suggested to be different. Here we report that crenactin forms bona fide double helical filaments that show exceptional similarity to eukaryotic F-actin. With cryo-electron microscopy and helical reconstruction we solved the structure of the crenactin filament to 3.8 A resolution. When forming double filaments, the 'hydrophobic plug' loop in crenactin rearranges. Arcadin-2, also encoded by the arcade gene cluster, binds tightly with its C-terminus to the hydrophobic groove of crenactin. Binding is reminiscent of eukaryotic actin modulators such as cofilin and thymosin beta4 and arcadin-2 is a depolymeriser of crenactin filaments. Our work further supports the theory of shared ancestry of Eukaryotes and Crenarchaea. | ||
| - | + | Crenactin forms actin-like double helical filaments regulated by arcadin-2.,Izore T, Kureisaite-Ciziene D, McLaughlin SH, Lowe J Elife. 2016 Nov 17;5. pii: e21600. doi: 10.7554/eLife.21600. PMID:27852434<ref>PMID:27852434</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5ly3" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Izore, T]] | [[Category: Izore, T]] | ||
| + | [[Category: Lowe, J]] | ||
| + | [[Category: Actin]] | ||
| + | [[Category: Bacterial cytoskeleton]] | ||
| + | [[Category: Structural protein]] | ||
Revision as of 18:37, 10 December 2016
P. calidifontis crenactin in complex with arcadin-2 C-terminal peptide
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