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Cited by 190

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase.

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Keitel, T, Simon, O, Borriss, R, Heinemann, U·1993·Proceedings of the National Academy of Sciences

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.

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Metadata

Authors
Keitel, T., Simon, O., Borriss, R., & Heinemann, U.
Venue
Proceedings of the National Academy of Sciences
Published
1993-06
Volume
90
Issue
11
Pages
5287-5291
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2129728418
Cited by
190
References
1
FWCI
17.40
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase. https://app.cochat.ai/papers/10.1073/pnas.90.11.5287
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Keitel, T., Simon, O., Borriss, R., & Heinemann, U. (1993). Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.90.11.5287

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