PDBsum entry: 2w39

Hydrolase

PDB id: 2w39

Contents

Protein chain

298 a.a. *

Ligands

NAG

BGC-LGC-BGC

Waters ×436

* Residue conservation analysis

PDB id:

2w39

Name:

Hydrolase

Title:

Glc(beta-1-3)glc disaccharide in -1 and -2 sites of laminarinase 16a from phanerochaete chrysosporium

Structure:

Putative laminarinase. Chain: a. Fragment: residues 21-318. Synonym: laminarinase 16a. Engineered: yes

Source:

Phanerochaete chrysosporium. Organism_taxid: 5306. Strain: k-3. Expressed in: pichia pastoris. Expression_system_taxid: 4922.

Resolution:

1.10Å R-factor: 0.138 R-free: 0.152

Authors:

J.Vasur,R.Kawai,E.Andersson,K.Igarashi,M.Sandgren, M.Samejima,J.Stahlberg

Key ref:

J.Vasur et al. (2009). X-ray crystal structures of Phanerochaete chrysosporium Laminarinase 16A in complex with products from lichenin and laminarin hydrolysis. FEBS J, 276, 3858-3869. PubMed id: 19769746

Date:

07-Nov-08 Release date: 21-Jul-09

Protein chain

Q874E3  (Q874E3_PHACH) -  Putative laminarinase

Seq: 318 a.a.

Struc: 298 a.a.

 Gene Ontology (GO) functional annotation 

• Biological process: carbohydrate metabolic process (1 term)
• Biochemical function: hydrolase activity, hydrolyzing O-glycosyl compounds (1 term)

FEBS J 276:3858-3869 (2009)

PubMed id: 19769746

X-ray crystal structures of Phanerochaete chrysosporium Laminarinase 16A in complex with products from lichenin and laminarin hydrolysis.

J.Vasur, R.Kawai, E.Andersson, K.Igarashi, M.Sandgren, M.Samejima, J.Ståhlberg.

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.