Structural characterization of a novel autonomous cohesin from Ruminococcus flavefaciens

Milana Voronov-Goldman, Maly Levy-Assaraf, Oren Yaniv, Gloria Wisserman, Sadanari Jindou, Ilya Borovok, Edward A. Bayer, Raphael Lamed, Linda J.W. Shimon*, Felix Frolow

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

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, ZP06142108), 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 -helical elements and a topographical protuberance on the putative dockerin-binding surface.

Original languageEnglish
Pages (from-to)450-456
Number of pages7
JournalActa Crystallographica Section F:Structural Biology Communications
Volume70
Issue number4
DOIs
StatePublished - Apr 2014

Keywords

  • cellulose degradation
  • cellulosome
  • cohesin-dockerin interaction
  • glycoside hydrolases
  • scaffoldin

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