TY - JOUR
T1 - Structural characterization of a novel autonomous cohesin from Ruminococcus flavefaciens
AU - Voronov-Goldman, Milana
AU - Levy-Assaraf, Maly
AU - Yaniv, Oren
AU - Wisserman, Gloria
AU - Jindou, Sadanari
AU - Borovok, Ilya
AU - Bayer, Edward A.
AU - Lamed, Raphael
AU - Shimon, Linda J.W.
AU - Frolow, Felix
PY - 2014/4
Y1 - 2014/4
N2 - 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.
AB - 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.
KW - cellulose degradation
KW - cellulosome
KW - cohesin-dockerin interaction
KW - glycoside hydrolases
KW - scaffoldin
UR - http://www.scopus.com/inward/record.url?scp=84905500966&partnerID=8YFLogxK
U2 - 10.1107/S2053230X14004051
DO - 10.1107/S2053230X14004051
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AN - SCOPUS:84905500966
SN - 1744-3091
VL - 70
SP - 450
EP - 456
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
IS - 4
ER -