TAILIEUCHUNG - Báo cáo khoa học: Kinetic and crystallographic analyses of the catalytic domain of chitinase from Pyrococcus furiosus – the role of conserved residues in the active site

The hyperthermostable chitinase from the hyperthermophilic archaeon Pyrococcus furiosushas a unique multidomain structure containing two chi-tin-binding domains and two catalytic domains, and exhibits strong crystal-line chitin hydrolyzing activity at high temperature. | ỊFEBS Journal Kinetic and crystallographic analyses of the catalytic domain of chitinase from Pyrococcus furiosus - the role of conserved residues in the active site Hiroaki Tsuji1 Shigenori Nishimura1 Takashi Inui1 Yuji Kado2 Kazuhiko Ishikawa2 Tsutomu Nakamura2 and Koichi Uegaki2 1 Laboratory of Protein Sciences Graduate Schoolof Life and EnvironmentalSciences Osaka Prefecture University Japan 2 NationalInstitute of Advanced IndustrialScience and Technology Osaka Japan Keywords chitinase crystal structure DXDXE motif glycoside hydrolase family Pyrococcus furiosus Correspondence S. Nishimura Laboratory of Protein Sciences Graduate School of Life and Environmental Sciences Osaka Prefecture University 1-1 Gakuencho Sakai Osaka 599-8531 Japan Fax 81 72 254 9462 Tel 81 72 254 9462 E-mail tigers@ K. Uegaki NationalInstitute of Advanced IndustrialScience and Technology 1-8-31 Midorigaoka Ikeda Osaka 563-8577 Japan Fax 81 72 751 8370 Tel 81 72 751 9526 E-mail k-uegaki@ Database Structural data are available at the Protein Data Bank under the accession numbers 3A4W E526A-substrate complex 3A4X D524A-substrate complex and 3AFB D524A apo-form Received 25 February 2010 revised 10 April 2010 accepted 13 April 2010 doi The hyperthermostable chitinase from the hyperthermophilic archaeon Pyrococcus furiosus has a unique multidomain structure containing two chitin-binding domains and two catalytic domains and exhibits strong crystalline chitin hydrolyzing activity at high temperature. In order to investigate the structure-function relationship of this chitinase we analyzed one of the catalytic domains AD2 using mutational and kinetic approaches and determined the crystal structure of AD2 complexed with chito-oligosaccha-ride substrate. Kinetic studies showed that among the acidic residues in the signature sequence of family 18 chitinases DXDXE motif the second Asp D2 and Glu E residues play critical roles in the .

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