Structure of the catalytic domain of the Clostridium thermocellum cellulase CelT

Acta Crystallographica. Section D, Biological Crystallography
Muppuru M KesavuluChwan Deng Hsiao

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.

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Citations

Oct 15, 2013·Journal of Synchrotron Radiation·Takao ArimoriTaro Tamada
Dec 30, 2014·Protein Science : a Publication of the Protein Society·Hiroyuki OkanoShigenori Kanaya
Oct 15, 2013·FEMS Microbiology Reviews·Sara E Blumer-SchuetteRobert M Kelly
Jul 4, 2018·Acta Crystallographica. Section D, Structural Biology·Thomas L EllinghausPaul D Adams
Jan 5, 2019·Chembiochem : a European Journal of Chemical Biology·Wen-Yih JengAndrew H-J Wang

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