1gqi

Structure of Pseudomonas cellulosa alpha-D-glucuronidase

spinqualitylabelsall models 1gqi, resolution 1.48Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1gqi is a 2 chain structure with sequence from Cellvibrio japonicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.48Å Ligands: CO, EDO, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AGUA_CELJU Alpha-glucuronidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. It catalyzes the cleavage of the alpha-1,2-glycosidic bond at the non-reducing end of 4-O-methyl-D-glucuronic acid (4-O-MeGlcA) side chain of short xylooligosaccharides and releases 4-O-methylglucuronic acid. It can also hydrolyze small soluble oligosaccharides such as dobiouronic acid, aldotriouronic acid, aldotetraouronic acid, and aldopentaouronic acid. 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 Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. The structure of the alpha-glucuronidase, GlcA67A, from Pseudomonas cellulosa reveals three domains, the central of which is a (beta/alpha)(8) barrel housing the catalytic apparatus. Complexes of the enzyme with the individual reaction products, either xylobiose or glucuronic acid, and the ternary complex of both glucuronic acid and xylotriose reveal a "blind" pocket which selects for short decorated xylooligosaccharides substituted with the uronic acid at their nonreducing end, consistent with kinetic data. The catalytic center reveals a constellation of carboxylates; Glu292 is poised to provide protonic assistance to leaving group departure with Glu393 and Asp365 both appropriately positioned to provide base-catalyzed assistance for inverting nucleophilic attack by water. The structural basis for catalysis and specificity of the Pseudomonas cellulosa alpha-glucuronidase, GlcA67A.,Nurizzo D, Nagy T, Gilbert HJ, Davies GJ Structure. 2002 Apr;10(4):547-56. PMID:11937059 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glucuronisidase 3D structures

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