1aq0

BARLEY 1,3-1,4-BETA-GLUCANASE IN MONOCLINIC SPACE GROUP

spinqualitylabelsall models 1aq0, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1aq0 is a 2 chain structure with sequence from Hordeum vulgare. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: ACT, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GUB2_HORVU Functions in plant cell wall hydrolysis during mobilization of the endosperm in germinating grain or during the growth of vegetative tissues. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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.,Muller JJ, Thomsen KK, Heinemann U J Biol Chem. 1998 Feb 6;273(6):3438-46. PMID:9452466 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glucanase 3D structures

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