1BYH

MOLECULAR AND ACTIVE-SITE STRUCTURE OF A BACILLUS (1-3,1-4)-BETA-GLUCANASE

Summary for 1BYH

• Entry DOI: 10.2210/pdb1byh/pdb
• Related PRD ID: PRD_900005
• Descriptor: HYBRID, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: hydrolase
• Biological source: synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 24375.73

Authors

Keitel, T.,Heinemann, U. (deposition date: 1992-12-31, release date: 1993-10-31, Last modification date: 2024-10-30)

Primary citation

Keitel, T.,Simon, O.,Borriss, R.,Heinemann, U.
Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase.
Proc.Natl.Acad.Sci.USA, 90:5287-5291, 1993

PubMed Abstract: The three-dimensional structure of the hybrid Bacillus 1,3-1,4-beta-glucanase (beta-glucanase; 1,3-1,4-beta-D-glucan 4-glucanohydrolase, lichenase, EC 3.2.1.73) designated H(A16-M) was determined by x-ray crystallography at a resolution of 2.0 A and refined to an R value of 16.4% using stereochemical restraints. The protein molecule consists mainly of two seven-stranded antiparallel beta-pleated sheets arranged atop each other to form a compact, sandwich-like structure. A channel crossing one side of the protein molecule accommodates an inhibitor, 3,4-epoxybutyl beta-D-cellobioside, which binds covalently to the side chain of Glu-105, as seen in a crystal structure analysis at 2.8-A resolution of the protein-inhibitor complex (R = 16.8%). That Glu-105 may be indispensible for enzyme catalysis by H(A16-M) is suggested by site-directed mutagenesis of this residue, which inevitably leads to an inactive enzyme.

PubMed: 8099449
DOI: 10.1073/pnas.90.11.5287

Experimental method

X-RAY DIFFRACTION (2.8 Å)