Vasur, Jonas
- Institutionen för molekylärbiologi, Sveriges lantbruksuniversitet
Forskningsartikel2009Vetenskapligt granskad
Vasur, Jonas; Kawai, Rie; Andersson, Evalena; Igarashi, Kiyohiko; Sandgren, Mats; Samejima, Masahiro; Ståhlberg, Jerry
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.
1; 3(4)-beta-d-glucanase; 3D protein-ligand structure; glycoside hydrolase family 16; laminarin; lichenin
FEBS Journal
2009, Volym: 276, nummer: 14, sidor: 4282-4293
Utgivare: WILEY-BLACKWELL PUBLISHING, INC
Förnyelsebar bioenergi
DOI: https://doi.org/10.1111/j.1742-4658.2009.07099.x
https://res.slu.se/id/publ/49755