1gbg | pdb_00001gbg

From Proteopedia
Revision as of 13:47, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1gbg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gbg, resolution 1.8Å" /> '''BACILLUS LICHENIFORMI...)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigationJump to search

BACILLUS LICHENIFORMIS BETA-GLUCANASE

File:1gbg.gif


1gbg, resolution 1.8Å

Drag the structure with the mouse to rotate

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

Proteopedia Page Contributors and Editors (what is this?)

OCA