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Publication Abstract from PubMed

Anaerobic bacteria organize carbohydrate-active enzymes into a multi-component complex, the cellulosome, which degrades cellulose and hemicellulose highly efficiently. Genome sequencing of Ruminococcus flavefaciens FD-1 offers extensive information on the range and diversity of the enzymatic and structural components of the cellulosome. The R. flavefaciens FD-1 genome encodes over 200 dockerin-containing proteins, most of which are of unknown function. One of these modular proteins comprises a glycoside hydrolase family 5 catalytic module (GH5) linked to an unclassified carbohydrate-binding module (CBM-Rf1) and a dockerin. The novel CBM-Rf1 has been purified and crystallized. The crystals belonged to the trigonal space group R32:H. The CBM-Rf1 structure was determined by a multiple-wavelength anomalous dispersion experiment using AutoSol from the PHENIX suite using both selenomethionyl-derivative and native data to resolutions of 2.28 and 2.0 A, respectively.

Expression, purification and crystallization of a novel carbohydrate-binding module from the Ruminococcus flavefaciens cellulosome.,Venditto I, Centeno MS, Ferreira LM, Fontes CM, Najmudin S Acta Crystallogr F Struct Biol Commun. 2014 Dec 1;70(Pt 12):1653-6. doi:, 10.1107/S2053230X14024248. Epub 2014 Nov 14. PMID:25484220^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.