Open AccessPreliminary X‐ray characterization of a novel type of anchoring cohesin from the cellulosome of Ruminococcus flavefaciens
Author(s) -
Alber Orly,
Noach Ilit,
Lamed Raphael,
Shimon Linda J. W.,
Bayer Edward A.,
Frolow Felix
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107067437
Subject(s) - cellulosome , ruminococcus , cohesin , chemistry , cell wall , biochemistry , biology , bacteria , crystallography , clostridium thermocellum , cellulase , stereochemistry , enzyme , dna , genetics , chromatin
Ruminococcus flavefaciens is an anaerobic bacterium that resides in the gastrointestinal tract of ruminants. It produces a highly organized multi‐enzyme cellulosome complex that plays a key role in the degradation of plant cell walls. ScaE is one of the critical structural components of its cellulosome that serves to anchor the complex to the cell wall. The seleno‐ l ‐methionine‐labelled derivative of the ScaE cohesin module has been cloned, expressed, purified and crystallized. The crystals belong to space group C 2, with unit‐cell parameters a = 155.6, b = 69.3, c = 93.0 Å, β = 123.4°, and contain four molecules in the asymmetric unit. Diffraction data were phased to 1.95 Å using the anomalous signal from the Se atoms.