1GQI

Structure of Pseudomonas cellulosa alpha-D-glucuronidase

Summary for 1GQI

• Entry DOI: 10.2210/pdb1gqi/pdb
• Related: 1GQJ 1GQK 1GQL
• Descriptor: ALPHA-GLUCURONIDASE, 1,2-ETHANEDIOL, COBALT (II) ION, ... (5 entities in total)
• Functional Keywords: glucuronidase, (alpha-beta)8 barrel, glycoside hydrolase
• Biological source: PSEUDOMONAS CELLULOSA
• Total number of polymer chains: 2
• Total formula weight: 162144.08

Authors

Nurizzo, D.,Nagy, T.,Gilbert, H.J.,Davies, G.J. (deposition date: 2001-11-26, release date: 2002-09-26, Last modification date: 2024-05-08)

Primary citation

Nurizzo, D.,Nagy, T.,Gilbert, H.J.,Davies, G.J.
The Structural Basis for Catalysis and Specificity of the Pseudomonas Cellulosa Alpha-Glucuronidase, Glca67A
Structure, 10:547-, 2002

PubMed Abstract: 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.

PubMed: 11937059
DOI: 10.1016/S0969-2126(02)00742-6

Experimental method

X-RAY DIFFRACTION (1.48 Å)