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Crystal structure of Bacillus licheniformis 1,3‐1,4‐β‐ d ‐glucan 4‐glucanohydrolase at 1.8 Å resolution
Author(s) -
Hahn Michael,
Pons Jaume,
Planas Antoni,
Querol Enrique,
Heinemann Udo
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01111-q
Subject(s) - bacillus licheniformis , glucan , chemistry , bacillaceae , crystal (programming language) , bacillus (shape) , resolution (logic) , bacillales , crystal structure , thermophile , enzyme , beta glucan , crystallography , bacteria , biochemistry , microbiology and biotechnology , biology , genetics , artificial intelligence , bacillus subtilis , computer science , programming language
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.