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

DOI: 10.1016/j.febslet.2014.01.029
PMID: 24486010

Authors: Thierry Izoré (MRC Laboratory of Molecular Biology) , Ramona Duman (Diamond Light Source) , Danguole Kureisaite-Ciziene (MRC Laboratory of Molecular Biology) , Jan Löwe (MRC Laboratory of Molecular Biology)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Letters , VOL 588 (5) , PAGES 776 - 782

State: Published (Approved)
Published: March 2014
Diamond Proposal Number(s): 8547

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.

Journal Keywords: Actin; MreB; Crenarchaea; Bacterial cytoskeleton; Helical filament; Cytomotive filament

Diamond Keywords: Archaea

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength)

Added On: 20/03/2014 12:53

Documents:
FEBS Letters - 2014 - Izor - Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms.pdf

Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)