Crystal structure of Bacillus licheniformis 1,3-1,4-β- d-glucan 4-glucanohydrolase at 1.8 Å 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 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.
- Publication:
-
FEBS Letters
- Pub Date:
- January 1995
- DOI:
- 10.1016/0014-5793(95)01111-Q
- Bibcode:
- 1995FEBSL.374..221H
- Keywords:
-
- 1;
- 3-1;
- 4-β- d-Glucan 4-glucanohydrolase;
- 1;
- 3-1;
- 4-β-Glucanase;
- Bacillus licheniformis;
- Crystal structure;
- β-Glucan hydrolysis;
- Enzyme mechanism;
- BGLL;
- 1;
- 3-1;
- 4-β-glucanase from Bacillus licheniformis;
- BGLM;
- 1;
- 3-1;
- 4-β-glucanase from Bacillus macerans;
- BGLA;
- 1;
- 3-1;
- 4-β-glucanase from Bacillus amylolique-faciens;
- H(A16-M);
- hybrid enzyme with amino acids 1–16 derived from BGLA and amino acids 17–214 from BGLM;
- PEG;
- polyethylene glycol;
- rms;
- root mean square