1BQC

BETA-MANNANASE FROM THERMOMONOSPORA FUSCA

Summary for 1BQC

• Entry DOI: 10.2210/pdb1bqc/pdb
• Descriptor: PROTEIN (BETA-MANNANASE) (2 entities in total)
• Functional Keywords: mannanase, glycosyl hydrolase, family 5, thermomonospora fusca, hydrolase
• Biological source: Thermobifida fusca
• Total number of polymer chains: 1
• Total formula weight: 33123.31

Authors

Hilge, M.,Gloor, S.M.,Piontek, K. (deposition date: 1998-08-12, release date: 1999-08-13, Last modification date: 2025-11-12)

Primary citation

Hilge, M.,Gloor, S.M.,Rypniewski, W.,Sauer, O.,Heightman, T.D.,Zimmermann, W.,Winterhalter, K.,Piontek, K.
High-resolution native and complex structures of thermostable beta-mannanase from Thermomonospora fusca - substrate specificity in glycosyl hydrolase family 5.
Structure, 6:1433-1444, 1998

PubMed Abstract: . beta-Mannanases hydrolyse the O-glycosidic bonds in mannan, a hemicellulose constituent of plants. These enzymes have potential use in pulp and paper production and are of significant biotechnological interest. Thermostable beta-mannanases would be particularly useful due to their high temperature optimum and broad pH tolerance. The thermophilic actinomycete Thermomonospora fusca secretes at least one beta-mannanase (molecular mass 38 kDa) with a temperature optimum of 80 degreesC. No three-dimensional structure of a mannan-degrading enzyme has been reported until now.

PubMed: 9817845
DOI: 10.1016/S0969-2126(98)00142-7

Experimental method

X-RAY DIFFRACTION (1.5 Å)