2W39

Glc(beta-1-3)Glc disaccharide in -1 and -2 sites of Laminarinase 16A from Phanerochaete chrysosporium

Summary for 2W39

• Entry DOI: 10.2210/pdb2w39/pdb
• Related: 2CL2
• Related PRD ID: PRD_900024
• Descriptor: PUTATIVE LAMINARINASE, beta-D-glucopyranose-(1-3)-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: phanerochaete chrysosporium, hydrolase, white rot fungus, glycosyl hydrolase, gh7, gh16, lam16a, laminarin, family 16, beta-glucan, basidiomycete, beta-glucanase, pichea pastoris, laminarinase, beta sandwich, extracellular
• Biological source: PHANEROCHAETE CHRYSOSPORIUM
• Total number of polymer chains: 1
• Total formula weight: 32664.37

Authors

Vasur, J.,Kawai, R.,Andersson, E.,Igarashi, K.,Sandgren, M.,Samejima, M.,Stahlberg, J. (deposition date: 2008-11-07, release date: 2009-07-21, Last modification date: 2024-11-13)

Primary citation

Vasur, J.,Kawai, R.,Andersson, E.,Igarashi, K.,Sandgren, M.,Samejima, M.,Stahlberg, J.
X-Ray Crystal Structures of Phanerochaete Chrysosporium Laminarinase 16A in Complex with Products from Lichenin and Laminarin Hydrolysis
FEBS J., 276:3858-, 2009

PubMed Abstract: The 1,3(4)-beta-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)-beta-D-glucanase Phanerochaete chrysosporium Laminarinase 16A in complex with beta-glucan products from laminarin (1.6 A) and lichenin (1.1 A) hydrolysis. The G6G3G3G glucan, in complex with the enzyme, showed a beta-1,6 branch in the acceptor site. The G4G3G ligand-protein complex showed that there was no room for a beta-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 beta-1,3 bond between them. These are the first X-ray crystal structures of any 1,3(4)-beta-D-glucanase in complex with glucan products. They provide details of both substrate and product binding in support of earlier enzymatic evidence.

PubMed: 19769746
DOI: 10.1111/J.1742-4658.2009.07099.X

Experimental method

X-RAY DIFFRACTION (1.1 Å)