1QOX

Beta-glucosidase from Bacillus circulans sp. alkalophilus

Summary for 1QOX

• Entry DOI: 10.2210/pdb1qox/pdb
• Descriptor: BETA-GLUCOSIDASE (2 entities in total)
• Functional Keywords: hydrolase, cellulose degradation
• Biological source: BACILLUS CIRCULANS
• Total number of polymer chains: 16
• Total formula weight: 819559.63

Authors

Hakulinen, N.,Rouvinen, J. (deposition date: 1999-11-24, release date: 2000-02-27, Last modification date: 2023-12-13)

Primary citation

Hakulinen, N.,Paavilainen, S.,Korpela, T.,Rouvinen, J.
The Crystal Structure of Beta-Glucosidase from Bacillus Circulans Sp. Alkalophilus: Ability to Form Long Polymeric Assemblies
J.Struct.Biol., 129:69-, 2000

PubMed Abstract: Family 1 of glycosyl hydrolases is a large and biologically important group of enzymes. A new three-dimensional structure of this family, beta-glucosidase from Bacillus circulans sp. alkalophilus is reported here. This is the first structure of beta-glucosidase from an alkaliphilic organism. The model was determined by the molecular replacement method and refined to a resolution of 2.7 A. The quaternary structure of B. circulans sp. alkalophilus beta-glucosidase is an octamer and subunits of the octamer show a similar (beta/alpha)(8) barrel fold to that previously reported for other family 1 enzymes. The crystal structure suggested that Cys169 in the active site is substituted. The Cys169 is located near the putative acid/base catalyst Glu166 and it may contribute to the high pH optimum of the enzyme. The crystal structure also revealed that the asymmetric unit contains two octamers which have a clear binding interaction with each other. The ability of the octamers to link with each other suggested that beta-glucosidase from Bacillus circulans sp. alkalophilus is able to form long polymeric assemblies, at least in the crystalline state.

PubMed: 10675298
DOI: 10.1006/JSBI.1999.4206

Experimental method

X-RAY DIFFRACTION (2.7 Å)