5ly3: Difference between revisions
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<StructureSection load='5ly3' size='340' side='right'caption='[[5ly3]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='5ly3' size='340' side='right'caption='[[5ly3]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ly3]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ly3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_calidifontis Pyrobaculum calidifontis] and [https://en.wikipedia.org/wiki/Pyrobaculum_calidifontis_JCM_11548 Pyrobaculum calidifontis JCM 11548]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5LY3 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
<tr id=' | <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></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ly3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ly3 OCA], [https://pdbe.org/5ly3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ly3 RCSB], [https://www.ebi.ac.uk/pdbsum/5ly3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ly3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/CREN1_PYRCJ CREN1_PYRCJ] Forms the backbone of an actin-like archaeal cytoskeleton, which is involved in cell shape determination. Has ATPase activity. Shows highest activity towards ATP or GTP as nucleotide, and only residual activity on UTP, CTP and dNTPs.<ref>PMID:21414041</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pyrobaculum calidifontis]] | ||
[[Category: | [[Category: Pyrobaculum calidifontis JCM 11548]] | ||
[[Category: | [[Category: Izore T]] | ||
[[Category: | [[Category: Lowe J]] | ||
Latest revision as of 13:56, 25 October 2023
P. calidifontis crenactin in complex with arcadin-2 C-terminal peptideP. calidifontis crenactin in complex with arcadin-2 C-terminal peptide
Structural highlights
FunctionCREN1_PYRCJ Forms the backbone of an actin-like archaeal cytoskeleton, which is involved in cell shape determination. Has ATPase activity. Shows highest activity towards ATP or GTP as nucleotide, and only residual activity on UTP, CTP and dNTPs.[1] Publication Abstract from PubMedThe 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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