Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Izore T, Duman R, Kureisaite-Ciziene D, Lowe J. Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments. FEBS Lett. 2014 Jan 28. pii: S0014-5793(14)00058-1. doi:, 10.1016/j.febslet.2014.01.029. PMID:24486010 doi:http://dx.doi.org/10.1016/j.febslet.2014.01.029
