Crystal structure of Bacillus licheniformis 1,3-1,4-β-d-glucan 4-glucanohydrolase at 1.8 Å resolution

Michael Hahn; Jaume Pons; Antoni Planas; Enrique Querol; Udo Heinemann

doi:10.1016/0014-5793(95)01111-Q

Crystal structure of Bacillus licheniformis 1,3-1,4-β-d-glucan 4-glucanohydrolase at 1.8 Å resolution

Michael Hahn, Jaume Pons, Antoni Planas, Enrique Querol, Udo Heinemann

Research output: Indexed journal article › Article › peer-review

78 Citations (Scopus)

Abstract

The crystal structure of the 1,3-1,4-β-d-glucan 4-glucanohydrolase from Bacillus licheniformis is solved at a resolution of 1.8 Å and refined to R = 16.5%. The protein has a similar β-sandwich structure as the homologous enzyme from Bacillus macerans and the hybrid H(A16-M). This demonstrates that the jellyroll fold of these proteins is remarkably rigid and only weakly influenced by crystal contacts. The crystal structure permits to extend mechanistic considerations derived for the B. licheniformis enzyme to the entire class of bacterial 1,3-1,4-β-d-glucan 4-glucanohydrolases.

Original language	English
Pages (from-to)	221-224
Number of pages	4
Journal	FEBS Letters
Volume	374
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(95)01111-Q
Publication status	Published - 30 Oct 1995

Keywords

1,3-1,4-β-Glucanase
1,3-1,4-β-d-Glucan 4-glucanohydrolase
Bacillus licheniformis
Crystal structure
Enzyme mechanism
β-Glucan hydrolysis

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10.1016/0014-5793(95)01111-Q

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@article{e8b77062159744229363594d22e4ecdb,

title = "Crystal structure of Bacillus licheniformis 1,3-1,4-β-d-glucan 4-glucanohydrolase at 1.8 {\AA} resolution",

abstract = "The crystal structure of the 1,3-1,4-β-d-glucan 4-glucanohydrolase from Bacillus licheniformis is solved at a resolution of 1.8 {\AA} and refined to R = 16.5%. The protein has a similar β-sandwich structure as the homologous enzyme from Bacillus macerans and the hybrid H(A16-M). This demonstrates that the jellyroll fold of these proteins is remarkably rigid and only weakly influenced by crystal contacts. The crystal structure permits to extend mechanistic considerations derived for the B. licheniformis enzyme to the entire class of bacterial 1,3-1,4-β-d-glucan 4-glucanohydrolases.",

keywords = "1,3-1,4-β-Glucanase, 1,3-1,4-β-d-Glucan 4-glucanohydrolase, Bacillus licheniformis, Crystal structure, Enzyme mechanism, β-Glucan hydrolysis",

author = "Michael Hahn and Jaume Pons and Antoni Planas and Enrique Querol and Udo Heinemann",

note = "Funding Information: Acknowledgements.{"} X-ray diffraction data used in this study were collected in the laboratory of Prof. W. Saenger (Freie Universit~t Berlin, Germany). Supported by the Deutsche Forschungsgemeinschaft (He 131819) and the Fonds der Chemischen Industrie.",

year = "1995",

month = oct,

day = "30",

doi = "10.1016/0014-5793(95)01111-Q",

language = "English",

volume = "374",

pages = "221--224",

journal = "FEBS Letters",

issn = "0014-5793",

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T1 - Crystal structure of Bacillus licheniformis 1,3-1,4-β-d-glucan 4-glucanohydrolase at 1.8 Å resolution

AU - Hahn, Michael

AU - Pons, Jaume

AU - Planas, Antoni

AU - Querol, Enrique

AU - Heinemann, Udo

N1 - Funding Information: Acknowledgements." X-ray diffraction data used in this study were collected in the laboratory of Prof. W. Saenger (Freie Universit~t Berlin, Germany). Supported by the Deutsche Forschungsgemeinschaft (He 131819) and the Fonds der Chemischen Industrie.

PY - 1995/10/30

Y1 - 1995/10/30

N2 - The crystal structure of the 1,3-1,4-β-d-glucan 4-glucanohydrolase from Bacillus licheniformis is solved at a resolution of 1.8 Å and refined to R = 16.5%. The protein has a similar β-sandwich structure as the homologous enzyme from Bacillus macerans and the hybrid H(A16-M). This demonstrates that the jellyroll fold of these proteins is remarkably rigid and only weakly influenced by crystal contacts. The crystal structure permits to extend mechanistic considerations derived for the B. licheniformis enzyme to the entire class of bacterial 1,3-1,4-β-d-glucan 4-glucanohydrolases.

AB - The crystal structure of the 1,3-1,4-β-d-glucan 4-glucanohydrolase from Bacillus licheniformis is solved at a resolution of 1.8 Å and refined to R = 16.5%. The protein has a similar β-sandwich structure as the homologous enzyme from Bacillus macerans and the hybrid H(A16-M). This demonstrates that the jellyroll fold of these proteins is remarkably rigid and only weakly influenced by crystal contacts. The crystal structure permits to extend mechanistic considerations derived for the B. licheniformis enzyme to the entire class of bacterial 1,3-1,4-β-d-glucan 4-glucanohydrolases.

KW - 1,3-1,4-β-Glucanase

KW - 1,3-1,4-β-d-Glucan 4-glucanohydrolase

KW - Bacillus licheniformis

KW - Crystal structure

KW - Enzyme mechanism

KW - β-Glucan hydrolysis

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SN - 0014-5793

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IS - 2

ER -

Crystal structure of Bacillus licheniformis 1,3-1,4-β-d-glucan 4-glucanohydrolase at 1.8 Å resolution

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