4bql | pdb_00004bql
Crystal structure of archaeal actin
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 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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