Structural characterization of a novel autonomous cohesin from Ruminococcus flavefaciens

Ruminococcus flavefaciens is a cellulolytic bacterium found in the rumen of herbivores and produces one of the most elaborate and variable cellulosome systems. The structure of an R. flavefaciens protein (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.

Source: Acta Crystallographica Section F - March 25, 2014 Category: Biochemistry Authors: Voronov-Goldman, M.Levy-Assaraf, M.Yaniv, O.Wisserman, G.Jindou, S.Borovok, I.Bayer, E.A.Lamed, R.Shimon, L.J.W.Frolow, F. Tags: cellulosome scaffoldin cohesin-dockerin interaction cellulose degradation glycoside hydrolases structural communications Source Type: research