2YIK

Catalytic domain of Clostridium thermocellum CelT

Summary for 2YIK

• Entry DOI: 10.2210/pdb2yik/pdb
• Related: 2XE9
• Descriptor: ENDOGLUCANASE, CALCIUM ION, ZINC ION, ... (4 entities in total)
• Functional Keywords: hydrolase
• Biological source: CLOSTRIDIUM THERMOCELLUM
• Total number of polymer chains: 1
• Total formula weight: 68766.55

Authors

Tsai, J.-Y.,Kesavulu, M.M.,Hsiao, C.-D. (deposition date: 2011-05-16, release date: 2012-02-29, Last modification date: 2023-12-20)

Primary citation

Kesavulu, M.M.,Tsai, J.-Y.,Lee, H.-L.,Liang, P.-H.,Hsiao, C.-D.
Structure of the Catalytic Domain of the Clostridium Thermocellum Cellulase Celt
Acta Crystallogr.,Sect.D, 68:310-, 2012

PubMed Abstract: Cellulases hydrolyze cellulose, a major component of plant cell walls, to oligosaccharides and monosaccharides. Several Clostridium species secrete multi-enzyme complexes (cellulosomes) containing cellulases. C. thermocellum CelT, a family 9 cellulase, lacks the accessory module(s) necessary for activity, unlike most other family 9 cellulases. Therefore, characterization of the CelT structure is essential in order to understand its catalytic mechanism. Here, the crystal structure of free CelTΔdoc, the catalytic domain of CelT, is reported at 2.1 Å resolution. Its structure differs in several aspects from those of other family 9 cellulases. CelTΔdoc contains an additional α-helix, α-helices of increased length and two additional surface-exposed β-strands. It also contains three calcium ions instead of one as found in C. cellulolyticum Cel9M. CelTΔdoc also has two flexible loops at the open end of its active-site cleft. Movement of these loops probably allows the substrate to access the active site. CelT is stable over a wide range of pH and temperature conditions, suggesting that CelT could be used to convert cellulose biomass into biofuel.

PubMed: 22349233
DOI: 10.1107/S0907444912001990

Experimental method

X-RAY DIFFRACTION (2.1 Å)