4bql: Difference between revisions
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==Crystal structure of archaeal actin== | |||
=== | <StructureSection load='4bql' size='340' side='right' caption='[[4bql]], [[Resolution|resolution]] 3.34Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4bql]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_21063 Dsm 21063]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BQL 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>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4bql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bql OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bql RCSB], [http://www.ebi.ac.uk/pdbsum/4bql PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of the archaeal actin, crenactin, from the rod-shaped hyperthermophilic (optimal growth at 90 degrees C) crenarchaeon Pyrobaculum calidifontis is reported at 3.35 A resolution. Despite low amino-acid sequence identity, the three-dimensional structure of the protein monomer is highly similar to those of eukaryotic actin and the bacterial MreB protein. Crenactin-specific features are also evident, as well as elements that are shared between crenactin and eukaryotic actin but are not found in MreB. In the crystal, crenactin monomers form right-handed helices, demonstrating that the protein is capable of forming filament-like structures. Monomer interactions in the helix, as well as interactions between crenactin and ADP in the nucleotide-binding pocket, are resolved at the atomic level and compared with those of actin and MreB. The results provide insights into the structural and functional properties of a heat-stable archaeal actin and contribute to the understanding of the evolution of actin-family proteins in the three domains of life. | |||
Structure of crenactin, an archaeal actin homologue active at 90 degrees C.,Lindas AC, Chruszcz M, Bernander R, Valegard K Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):492-500. doi:, 10.1107/S1399004714000935. Epub 2014 Jan 30. PMID:24531483<ref>PMID:24531483</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
[[Category: Bernander, R | == References == | ||
[[Category: Chruszsz, M | <references/> | ||
[[Category: Lindaas, A C | __TOC__ | ||
[[Category: Valegard, K | </StructureSection> | ||
[[Category: Dsm 21063]] | |||
[[Category: Bernander, R]] | |||
[[Category: Chruszsz, M]] | |||
[[Category: Lindaas, A C]] | |||
[[Category: Valegard, K]] | |||
[[Category: Archaea]] | [[Category: Archaea]] | ||
[[Category: Contractile protein]] | [[Category: Contractile protein]] | ||
