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Expression, purification and crystallization of a novel carbohydrate-binding module from the

DOI: 10.1107/S2053230X14024248 DOI Help
PMID: 25484220 PMID Help

Authors: Immacolata Venditto (CIISA, Faculdade de Medicina Veterinaria, Universidade de Lisboa) , Maria S. J. Centeno (CIISA, Faculdade de Medicina Veterinaria, Universidade de Lisboa) , Luis M. A. Ferreira (CIISA, Faculdade de Medicina Veterinaria, Universidade de Lisboa) , Carlos M. G. A. Fontes (CIISA, Faculdade de Medicina Veterinaria, Universidade de Lisboa) , Shabir Najmudin (Universidade Técnica de Lisboa)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 70 , PAGES 1653 - 1656

State: Published (Approved)
Published: December 2014

Abstract: 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 Å, respectively.

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography

Other Facilities: ESRF (beamline ID29)

Added On: 06/02/2015 09:46

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