Published in

International Union of Crystallography, Acta Crystallographica Section F: Structural Biology Communications, 4(70), p. 450-456, 2014

DOI: 10.1107/s2053230x14004051

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Structural characterization of a novel autonomous cohesin fromRuminococcus flavefaciens

This paper is available in a repository.
This paper is available in a repository.

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Abstract

Ruminococcus flavefaciensis a cellulolytic bacterium found in the rumen of herbivores and produces one of the most elaborate and variable cellulosome systems. The structure of anR. flavefaciensprotein (RfCohG, ZP_06142108), representing a freestanding (non-cellulosomal) type III cohesin module, has been determined. A selenomethionine derivative with a C-terminal histidine tag was crystallized and diffraction data were measured to 2.44 Å resolution. Its structure was determined by single-wavelength anomalous dispersion, revealing eight molecules in the asymmetric unit.RfCohG exhibits the most complex among all known cohesin structures, possessing four α-helical elements and a topographical protuberance on the putative dockerin-binding surface.