View source for 4bql


==Crystal structure of archaeal actin==
<StructureSection load='4bql' size='340' side='right'caption='[[4bql]], [[Resolution|resolution]] 3.34&Aring;' 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://pdbe.org/4bql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bql RCSB], [http://www.ebi.ac.uk/pdbsum/4bql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bql ProSAT]</span></td></tr>
</table>
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Dsm 21063]]
[[Category: Large Structures]]
[[Category: Bernander, R]]
[[Category: Chruszsz, M]]
[[Category: Lindaas, A C]]
[[Category: Valegard, K]]
[[Category: Archaea]]
[[Category: Contractile protein]]
[[Category: Crenarchaeota]]
[[Category: Cytoskeleton]]
[[Category: Evolution]]