1gbg
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(New page: 200px<br /><applet load="1gbg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gbg, resolution 1.8Å" /> '''BACILLUS LICHENIFORMI...)
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Revision as of 13:47, 20 November 2007
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BACILLUS LICHENIFORMIS BETA-GLUCANASE
Overview
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.
About this Structure
1GBG is a Single protein structure of sequence from Bacillus licheniformis with CA as ligand. Active as Licheninase, with EC number 3.2.1.73 Full crystallographic information is available from OCA.
Reference
Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase at 1.8 A resolution., Hahn M, Pons J, Planas A, Querol E, Heinemann U, FEBS Lett. 1995 Oct 30;374(2):221-4. PMID:7589539
Page seeded by OCA on Tue Nov 20 15:54:15 2007
