5ly5
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Arcadin-1 from Pyrobaculum calidifontis== | |
+ | <StructureSection load='5ly5' size='340' side='right'caption='[[5ly5]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5ly5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_calidifontis Pyrobaculum calidifontis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LY5 FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=5ly5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ly5 OCA], [https://pdbe.org/5ly5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ly5 RCSB], [https://www.ebi.ac.uk/pdbsum/5ly5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ly5 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/Q8ZVH7_PYRAE Q8ZVH7_PYRAE] | ||
+ | <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> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 5ly5" style="background-color:#fffaf0;"></div> |
- | [[Category: Izore | + | == References == |
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Pyrobaculum calidifontis]] | ||
+ | [[Category: Izore T]] | ||
+ | [[Category: Lowe J]] |
Current revision
Arcadin-1 from Pyrobaculum calidifontis
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