TAILIEUCHUNG - Báo cáo khoa học: New evidence for the role of calcium in the glycosidase reaction of GH43 arabinanases

Endo-1,5-a-l-arabinanases are glycosyl hydrolases that are able to cleave the glycosidic bonds of a-1,5-l-arabinan, releasing arabino-oligosaccharides and l-arabinose. Two extracellular endo-1,5-a-l-arabinanases have been isolated from Bacillus subtilis, BsArb43A and BsArb43B (formally named AbnA and Abn2, respectively). | New evidence for the role of calcium in the glycosidase reaction of GH43 arabinanases Daniele de Sanctis1 2 Jose M. Inácio1 f Peter F. Lindley Isabel de Sa-Nogueira1 3 and Isabel Bento1 1 Institute de Tecnologia Quimica e Biologica Universidade Nova de Lisboa Oeiras Portugal 2 StructuralBiology Group European Synchrotron Radiation Facility Grenoble France 3 Departamento de Ciencias da Vida Faculdade de Ciencias e Tecnologia Universidade Nova de Lisboa Caparica Portugal Keywords Bacillus subtilis catalytic mechanism crystallography endo-a-L-arabinananase GH43 mutagenesis Correspondence I. Bento Instituto de Tecnologia Quimica e Biologica Universidade Nova de Lisboa Avenida de Republica-EAN 2780-157 Oeiras Portugal Fax 351 21 441 1277 Tel 351 21 446 9100 E-mail bento@ I. de Sa-Nogueira Instituto de Tecnologia Química e Biológica Universidade Nova de Lisboa Avenida de Republica-EAN 2780-157 Oeiras Portugal Fax 351 21 441 1277 Tel 351 21 446 9100 E-mail sanoguei@ EWo-1 5-a-L-arabinanases are glycosyl hydrolases that are able to cleave the glycosidic bonds of a-1 5-L-arabinan releasing arabino-oligosaccharides and L-arabinose. Two extracellular endo-1 5-a-L-arabinanases have been isolated from Bacillus subtilis BsArb43A and BsArb43B formally named AbnA and Abn2 respectively . BsArb43B shows low sequence identity with previously characterized 1 5-a-L-arabinanases and is a much larger enzyme. Here we describe the 3D structure of native BsArb43B biochemical and structure characterization of two BsArb43B mutant proteins H318A and D171A and the 3D structure of the BsArb43B D171A mutant enzyme in complex with arabinohexose. The 3D structure of BsArb43B is different from that of other structurally characterized endo-1 5-a-L-arabinanases as it comprises two domains an N-terminal catalytic domain with a 3D fold similar to that observed for other endo-1 5-a-L-arabinanases and an additional C-terminal domain. Moreover this work also provides experimental .

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