4cj7

Structure of Crenactin, an archeal actin-like protein

spinqualitylabelsall models 4cj7, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cj7 is a 2 chain structure with sequence from Pyrobaculum calidifontis JCM 11548. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.2Å Ligands: ADP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. Publication Abstract from PubMed Polymerising proteins of the actin family are nearly ubiquitous. Crenactins, restricted to Crenarchaea, are more closely related to actin than bacterial MreB. Crenactins occur in gene clusters hinting at an unknown, but conserved function. We solved the crystal structure of crenactin at 3.2A resolution. The protein crystallises as a continuous right-handed helix with 8 subunits per complete turn, spanning 419A. The structure of crenactin shows several loops that are longer than in actin, but overall, crenactin is closely related to eukaryotic actin, with an RMSD of 1.6A. Crenactin filaments imaged by electron microscopy showed polymers with very similar helical parameters. Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments.,Izore T, Duman R, Kureisaite-Ciziene D, Lowe J FEBS Lett. 2014 Jan 28. pii: S0014-5793(14)00058-1. doi:, 10.1016/j.febslet.2014.01.029. PMID:24486010 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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