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PDBsum entry 1ayh
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References listed in PDB file
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Key reference
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Title
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Molecular and active-Site structure of a bacillus 1,3-1,4-Beta-Glucanase.
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Authors
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T.Keitel,
O.Simon,
R.Borriss,
U.Heinemann.
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Ref.
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Proc Natl Acad Sci U S A, 1993,
90,
5287-5291.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Hybrid bacillus (1-3,1-4)-Beta-Glucanases: engineering thermostable enzymes by construction of hybrid genes.
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Authors
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O.Olsen,
R.Borriss,
O.Simon,
K.K.Thomsen.
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Ref.
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Mol Gen Genet, 1991,
225,
177-185.
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PubMed id
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