TAILIEUCHUNG - Báo cáo khoa học: X-ray crystal structures of Phanerochaete chrysosporium Laminarinase 16A in complex with products from lichenin and laminarin hydrolysis

The 1,3(4)-b-d-glucanases of glycoside hydrolase family 16 provide useful examples of versatile yet specific protein–carbohydrate interactions. In the present study, we report the X-ray structures of the 1,3(4)-b-d-glucanase Phanerochaete chrysosporiumLaminarinase 16A in complex withb-glucan products from laminarin ( A˚ ) and lichenin ( A ˚ ) hydrolysis. The G6G3G3G glucan, in complex with the enzyme, showed ab-1,6 branch in the acceptor site. | X-ray crystal structures of Phanerochaete chrysosporium Laminarinase 16A in complex with products from lichenin and laminarin hydrolysis Jonas Vasur1 Rie Kawai2 Evalena Andersson1 Kiyohiko Igarashi2 Mats Sandgren1 Masahiro Samejima2 and Jerry Stahlberg1 1 Department of Molecular Biology University of AgriculturalSciences Uppsala Sweden 2 Department of BiomaterialSciences Graduate Schoolof Agriculture and Life Sciences The University of Tokyo Japan Keywords I 3 4 -P-D-glucanase 3D protein-ligand structure glycoside hydrolase family 16 laminarin lichenin Correspondence J. Stahlberg Department of Molecular Biology University of AgriculturalSciences Box 590 SE-75124 Uppsala Sweden Fax 46 18 536971 Tel 46 18 471 4590 E-mail jerry@ Note The models and electron density maps of enzyme-substrate complexes have been deposited in the Protein Data Bank 51 and in the Electron Density Server 52 with accession codes 2W39 and 2W52 Received 27 March 2009 revised 21 April 2009 accepted 14 May 2009 doi The 1 3 4 -P-D-glucanases of glycoside hydrolase family 16 provide useful examples of versatile yet specific protein-carbohydrate interactions. In the present study we report the X-ray structures of the 1 3 4 -P-D-glucanase Phanerochaete chrysosporium Laminarinase 16A in complex with P-glucan products from laminarin A and lichenin A hydrolysis. The G6G3G3G glucan in complex with the enzyme showed a P-1 6 branch in the acceptor site. The G4G3G ligand-protein complex showed that there was no room for a P-1 6 branch in the -1 or -2 subsites furthermore the distorted residue in the -1 subsite and the glucose in the -2 subsite required a P-1 3 bond between them. These are the first X-ray crystal structures of any 1 3 4 -P-D-glucanase in complex with glucan products. They provide details of both substrate and product binding in support of earlier enzymatic evidence. Introduction Glucan architecture is determined by the pattern of .

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