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| | <SX load='5mw1' size='340' side='right' viewer='molstar' caption='[[5mw1]], [[Resolution|resolution]] 3.80Å' scene=''> | | <SX load='5mw1' size='340' side='right' viewer='molstar' caption='[[5mw1]], [[Resolution|resolution]] 3.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5mw1]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_21063 Dsm 21063]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5ly4 5ly4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MW1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MW1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5mw1]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_calidifontis Pyrobaculum calidifontis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5ly4 5ly4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MW1 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></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]] 3.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pcal_1635 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=181486 DSM 21063])</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></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5mw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mw1 OCA], [http://pdbe.org/5mw1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mw1 RCSB], [http://www.ebi.ac.uk/pdbsum/5mw1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mw1 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=5mw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mw1 OCA], [https://pdbe.org/5mw1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mw1 RCSB], [https://www.ebi.ac.uk/pdbsum/5mw1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mw1 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__ |
| | </SX> | | </SX> |
| - | [[Category: Dsm 21063]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Izore, T]] | + | [[Category: Pyrobaculum calidifontis]] |
| - | [[Category: Lowe, J]] | + | [[Category: Izore T]] |
| - | [[Category: Actin]] | + | [[Category: Lowe J]] |
| - | [[Category: Bacterial cytoskeleton]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ettema TJ, Lindas AC, Bernander R. An actin-based cytoskeleton in archaea. Mol Microbiol. 2011 May;80(4):1052-61. doi: 10.1111/j.1365-2958.2011.07635.x., Epub 2011 Apr 6. PMID:21414041 doi:http://dx.doi.org/10.1111/j.1365-2958.2011.07635.x
- ↑ Izore T, Kureisaite-Ciziene D, McLaughlin SH, Lowe J. Crenactin forms actin-like double helical filaments regulated by arcadin-2. Elife. 2016 Nov 17;5. pii: e21600. doi: 10.7554/eLife.21600. PMID:27852434 doi:http://dx.doi.org/10.7554/eLife.21600
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