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Structural characterization of a novel autonomous cohesin from Ruminococcus flavefaciens
Author(s) -
VoronovGoldman Milana,
LevyAssaraf Maly,
Yaniv Oren,
Wisserman Gloria,
Jindou Sadanari,
Borovok Ilya,
Bayer Edward A.,
Lamed Raphael,
Shimon Linda J. W.,
Frolow Felix
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14004051
Subject(s) - cellulosome , cohesin , ruminococcus , chemistry , rumen , biochemistry , biology , bacteria , crystallography , dna , cellulase , genetics , clostridium thermocellum , enzyme , chromatin , fermentation
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 ( Rf CohG, 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. Rf CohG exhibits the most complex among all known cohesin structures, possessing four α‐helical elements and a topographical protuberance on the putative dockerin‐binding surface.