4N2O

Structure of a novel autonomous cohesin protein from Ruminococcus flavefaciens

Summary for 4N2O

• Entry DOI: 10.2210/pdb4n2o/pdb
• Descriptor: Autonomous cohesin, CHLORIDE ION (3 entities in total)
• Functional Keywords: nine-stranded beta sandwich, cohesin, dockerin, structural protein
• Biological source: Ruminococcus flavefaciens
• Total number of polymer chains: 8
• Total formula weight: 182907.06

Authors

Frolow, F.,Voronov-Goldman, M.,Levy-Assaraf, M.,Lamed, R.,Bayer, E.,Shimon, L. (deposition date: 2013-10-05, release date: 2013-12-18, Last modification date: 2019-07-17)

Primary citation

Voronov-Goldman, M.,Levy-Assaraf, M.,Yaniv, O.,Wisserman, G.,Jindou, S.,Borovok, I.,Bayer, E.A.,Lamed, R.,Shimon, L.J.,Frolow, F.
Structural characterization of a novel autonomous cohesin from Ruminococcus flavefaciens.
Acta Crystallogr F Struct Biol Commun, 70:450-456, 2014

PubMed 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.

PubMed: 24699736
DOI: 10.1107/S2053230X14004051

Experimental method

X-RAY DIFFRACTION (2.442 Å)