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- Title
Crystallization and preliminary crystallographic studies of a novel noncatalytic carbohydrate-binding module from the Ruminococcus flavefaciens cellulosome.
- Authors
Venditto, Immacolata; Goyal, Arun; Thompson, Andrew; Ferreira, Luis M. A.; Fontes, Carlos M. G. A.; Najmudin, Shabir
- Abstract
Microbial degradation of the plant cell wall is a fundamental biological process with considerable industrial importance. Hydrolysis of recalcitrant polysaccharides is orchestrated by a large repertoire of carbohydrate-active enzymes that display a modular architecture in which a catalytic domain is connected via linker sequences to one or more noncatalytic carbohydrate-binding modules (CBMs). CBMs direct the appended catalytic modules to their target substrates, thus potentiating catalysis. The genome of the most abundant ruminal cellulolytic bacterium, Ruminococcus flavefaciens strain FD-1, provides an opportunity to discover novel cellulosomal proteins involved in plant cell-wall deconstruction. It encodes a modular protein comprising a glycoside hydrolase family 9 catalytic module (GH9) linked to two unclassified tandemly repeated CBMs (termed CBM- Rf6A and CBM- Rf6B) and a C-terminal dockerin. The novel CBM- Rf6A from this protein has been crystallized and data were processed for the native and a selenomethionine derivative to 1.75 and 1.5 Å resolution, respectively. The crystals belonged to orthorhombic and cubic space groups, respectively. The structure was solved by a single-wavelength anomalous dispersion experiment using the CCP4 program suite and SHELXC/ D/ E.
- Subjects
CRYSTALLIZATION; RUMINOCOCCUS flavefaciens; CARBOHYDRATE-binding proteins; HYDROLASES; AMINO acids
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2015, Vol 71, Issue 1, p45
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X14025576