Open AccessOverexpression, crystallization and preliminary X‐ray crystallographic analysis of glucuronoxylan xylanohydrolase (Xyn30A) from Clostridium thermocellum
Author(s) -
Verma Anil Kumar,
Goyal Arun,
Freire Filipe,
Bule Pedro,
Venditto Immacolata,
Brás Joana L. A.,
Santos Helena,
Cardoso Vânia,
Bonifácio Cecília,
Thompson Andrew,
Romão Maria João,
Prates José A. M.,
Ferreira Luís M. A.,
Fontes Carlos M. G. A.,
Najmudin Shabir
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113025050
Subject(s) - clostridium thermocellum , glycoside hydrolase , carbohydrate binding module , molecular mass , chemistry , cell wall , cellulosome , biochemistry , recombinant dna , molecular replacement , crystallography , crystallization , cellulase , protein structure , enzyme , stereochemistry , organic chemistry , gene
The modular carbohydrate‐active enzyme belonging to glycoside hydrolase family 30 (GH30) from Clostridium thermocellum ( Ct XynGH30) is a cellulosomal protein which plays an important role in plant cell‐wall degradation. The full‐length Ct XynGH30 contains an N‐terminal catalytic module (Xyn30A) followed by a family 6 carbohydrate‐binding module (CBM6) and a dockerin at the C‐terminus. The recombinant protein has a molecular mass of 45 kDa. Preliminary structural characterization was carried out on Xyn30A crystallized in different conditions. All tested crystals belonged to space group P 1 with one molecule in the asymmetric unit. Molecular replacement has been used to solve the Xyn30A structure.