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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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.