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 angstrom) and lichenin (1.1 angstrom) 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.

Keywords

1; 3(4)-beta-d-glucanase; 3D protein-ligand structure; glycoside hydrolase family 16; laminarin; lichenin

Published in

FEBS Journal
2009, Volume: 276, number: 14, pages: 4282-4293
Publisher: WILEY-BLACKWELL PUBLISHING, INC

SLU Authors

• Vasur, Jonas

  • Department of Molecular Biology, Swedish University of Agricultural Sciences
    

• Andersson, Evalena

  • Department of Molecular Biology, Swedish University of Agricultural Sciences
    

• Sandgren, Mats

  • Department of Molecular Biology, Swedish University of Agricultural Sciences
    

• Ståhlberg, Jerry

  • Department of Molecular Biology, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Renewable Bioenergy Research


Publication identifier

DOI: https://doi.org/10.1111/j.1742-4658.2009.07099.x

Permanent link to this page (URI)

https://res.slu.se/id/publ/49755