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• W2129728418 endingPage "5291" @default.
• W2129728418 startingPage "5287" @default.
• W2129728418 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." @default.
• W2129728418 created "2016-06-24" @default.
• W2129728418 creator A5011489783 @default.
• W2129728418 creator A5016984762 @default.
• W2129728418 creator A5041600015 @default.
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• W2129728418 date "1993-06-01" @default.
• W2129728418 modified "2023-10-09" @default.
• W2129728418 title "Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase." @default.
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• W2129728418 doi "https://doi.org/10.1073/pnas.90.11.5287" @default.
• W2129728418 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/46701" @default.
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