1GBG

BACILLUS LICHENIFORMIS BETA-GLUCANASE

Summary for 1GBG

• Entry DOI: 10.2210/pdb1gbg/pdb
• Descriptor: (1,3-1,4)-BETA-D-GLUCAN 4 GLUCANOHYDROLASE, CALCIUM ION (3 entities in total)
• Functional Keywords: hydrolase (glucanase)
• Biological source: Bacillus licheniformis
• Total number of polymer chains: 1
• Total formula weight: 24414.93

Authors

Hahn, M.,Heinemann, U. (deposition date: 1995-08-25, release date: 1995-12-07, Last modification date: 2024-11-20)

Primary citation

Hahn, M.,Pons, J.,Planas, A.,Querol, E.,Heinemann, U.
Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase at 1.8 A resolution.
FEBS Lett., 374:221-224, 1995

PubMed Abstract: The crystal structure of the 1,3-1,4-beta-D-glucan 4-glucanohydrolase from Bacillus licheniformis is solved at a resolution of 1.8 A and refined to R = 16.5%. The protein has a similar beta-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-beta-D-glucan 4-glucanohydrolases.

PubMed: 7589539
DOI: 10.1016/0014-5793(95)01111-Q

Experimental method

X-RAY DIFFRACTION (1.8 Å)