| Literature DB >> 24316849 |
Anil Kumar Verma1, Arun Goyal, Filipe Freire, Pedro Bule, Immacolata Venditto, Joana L A Brás, Helena Santos, Vânia Cardoso, Cecília Bonifácio, Andrew Thompson, Maria João Romão, José A M Prates, Luís M A Ferreira, Carlos M G A Fontes, Shabir Najmudin.
Abstract
The modular carbohydrate-active enzyme belonging to glycoside hydrolase family 30 (GH30) from Clostridium thermocellum (CtXynGH30) is a cellulosomal protein which plays an important role in plant cell-wall degradation. The full-length CtXynGH30 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 P1 with one molecule in the asymmetric unit. Molecular replacement has been used to solve the Xyn30A structure.Entities:
Keywords: Clostridium thermocellum; Xyn30A; glycoside hydrolase family 30
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Year: 2013 PMID： 24316849 PMCID： PMC3855739 DOI： 10.1107/S1744309113025050
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091