1AQ0
BARLEY 1,3-1,4-BETA-GLUCANASE IN MONOCLINIC SPACE GROUP
Summary for 1AQ0
| Entry DOI | 10.2210/pdb1aq0/pdb |
| Descriptor | 1,3-1,4-BETA-GLUCANASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | hydrolase, glycosidase, glycoprotein, glycosylated protein |
| Biological source | Hordeum vulgare |
| Total number of polymer chains | 2 |
| Total formula weight | 65249.53 |
| Authors | Mueller, J.J.,Thomsen, K.K.,Heinemann, U. (deposition date: 1997-08-05, release date: 1998-02-11, Last modification date: 2024-10-23) |
| Primary citation | Muller, J.J.,Thomsen, K.K.,Heinemann, U. Crystal structure of barley 1,3-1,4-beta-glucanase at 2.0-A resolution and comparison with Bacillus 1,3-1,4-beta-glucanase. J.Biol.Chem., 273:3438-3446, 1998 Cited by PubMed Abstract: Both plants and bacteria produce enzymes capable of degrading the mixed-linked beta-glucan of the endosperm cell walls of cereal grains. The enzymes share the specificity for beta-1,4 glycosyl bonds of O-3-substituted glucose units in linear polysaccharides and a similar cleavage mechanism but are unrelated in sequence and tertiary structure. The three-dimensional structure of the 1,3-1, 4-beta-glucanase isoenzyme EII from barley was determined from monoclinic crystals at a resolution of 2.0 A. The protein is folded into a betaalpha8 barrel structure as has been shown previously (Varghese, J. N., Garrett, T. P. J., Colman, P. M., Chen, L., Hoj, P. B., and Fincher, G. B. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 2785-2789) by diffraction analysis at lower resolution of tetragonal crystals. It contains one N-glycosylation site which is described in detail with the sugar moieties attached to residue Asn190. The geometry and hydration of the barley 1,3-1,4-beta-glucanase is analyzed; a model beta-glucan fragment is placed into the binding site by molecular dynamics simulation, and the beta-glucan binding grooves of the plant and bacterial enzymes are compared. Their active sites are shown to have a small number of common features in generally dissimilar geometries that serve to explain both the identical substrate specificity and the observed differences in inhibitor binding. PubMed: 9452466DOI: 10.1074/jbc.273.6.3438 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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