Structural characterization of a novel autonomous cohesin from Ruminococcus flavefaciens

Acta Crystallogr F Struct Biol Commun. 2014 Apr;70(Pt 4):450-6. doi: 10.1107/S2053230X14004051. Epub 2014 Mar 25.

Abstract

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.

Keywords: cellulose degradation; cellulosome; cohesin-dockerin interaction; glycoside hydrolases; scaffoldin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Cell Cycle Proteins / chemistry*
  • Cell Cycle Proteins / metabolism
  • Cellulosomes / chemistry*
  • Cellulosomes / metabolism
  • Chromosomal Proteins, Non-Histone / chemistry*
  • Chromosomal Proteins, Non-Histone / metabolism
  • Cohesins
  • Crystallization
  • Crystallography, X-Ray
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Ruminococcus / metabolism*
  • Selenomethionine / chemistry
  • Selenomethionine / metabolism
  • Sequence Homology, Amino Acid
  • Tyrosine / chemistry

Substances

  • Cell Cycle Proteins
  • Chromosomal Proteins, Non-Histone
  • Tyrosine
  • Selenomethionine

Associated data

  • PDB/4N2O