5H9Y

Crystal structure of GH family 64 laminaripentaose-producing beta-1,3-glucanase from Paenibacillus barengoltzii complexed with laminarihexaose.

Summary for 5H9Y

• Entry DOI: 10.2210/pdb5h9y/pdb
• Related: 5H9X
• Descriptor: beta-1,3-glucanase, beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose, beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: beta-1, 3-glucan recognition, glycoside hydrolase family 64, 3-glucanase, gh64-tlp-sf superfamily, hydrolase
• Biological source: Paenibacillus barengoltzii
• Total number of polymer chains: 1
• Total formula weight: 50663.20

Authors

Zhen, Q.,Yan, Q.,Yang, S.,Jiang, Z.,You, X. (deposition date: 2015-12-29, release date: 2017-02-15, Last modification date: 2023-11-08)

Primary citation

Qin, Z.,Yang, D.,You, X.,Liu, Y.,Hu, S.,Yan, Q.,Yang, S.,Jiang, Z.
The recognition mechanism of triple-helical beta-1,3-glucan by a beta-1,3-glucanase
Chem. Commun. (Camb.), 53:9368-9371, 2017

PubMed Abstract: β-1,3-Glucan is one of the most abundant polysaccharides in fungi. Recognition of β-1,3-glucan occurs in both hydrolysis by glycoside hydrolases and immunological recognition. Our study provides a novel structural account of how glycoside hydrolase recognizes and hydrolyzes substrates in a triple-helical form and presents a general structural basis of β-1,3-glucan recognition.

PubMed: 28787048
DOI: 10.1039/c7cc03330c

Experimental method

X-RAY DIFFRACTION (1.969 Å)