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FEBS Lett. 2014 Mar 3;588(5):776-82. doi: 10.1016/j.febslet.2014.01.029. Epub 2014 Jan 28.

Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments.

Author information

1
MRC Laboratory of Molecular Biology, Structural Studies Division, Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom.
2
MRC Laboratory of Molecular Biology, Structural Studies Division, Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom. Electronic address: jyl@mrc-lmb.cam.ac.uk.

Abstract

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 3.2 Å resolution. The protein crystallises as a continuous right-handed helix with 8 subunits per complete turn, spanning 419 Å. 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 1.6 Å. Crenactin filaments imaged by electron microscopy showed polymers with very similar helical parameters.

KEYWORDS:

Actin; Bacterial cytoskeleton; Crenarchaea; Cytomotive filament; Helical filament; MreB

PMID:
24486010
PMCID:
PMC4158420
DOI:
10.1016/j.febslet.2014.01.029
[Indexed for MEDLINE]
Free PMC Article

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