1h41
From Proteopedia
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PSEUDOMONAS CELLULOSA E292A ALPHA-D-GLUCURONIDASE MUTANT COMPLEXED WITH ALDOTRIURONIC ACID
Overview
alpha-Glucuronidases are key components of the ensemble of enzymes that, degrade the plant cell wall. They hydrolyze the alpha1,2-glycosidic bond, between 4-O-methyl-d-glucuronic acid (4-O-MeGlcA) and the xylan or, xylooligosaccharide backbone. Here we report the crystal structure of an, inactive mutant (E292A) of the alpha-glucuronidase, GlcA67A, from, Cellvibrio japonicus in complex with its substrate. The data show that the, 4-O-methyl group of the substrate is accommodated within a hydrophobic, sheath flanked by Val-210 and Trp-160, whereas the carboxylate moiety is, located within a positively charged region of the substrate-binding, pocket. The carboxylate side chains of Glu-393 and Asp-365, on the, "beta-face" of 4-O-MeGlcA, form hydrogen bonds with a water molecule that, is ... [(full description)]
About this Structure
1H41 is a [Single protein] structure of sequence from [Cellvibrio japonicus] with GCV, CO and EDO as [ligands]. Active as [Alpha-glucuronidase], with EC number [3.2.1.139]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
The alpha-glucuronidase, GlcA67A, of Cellvibrio japonicus utilizes the carboxylate and methyl groups of aldobiouronic acid as important substrate recognition determinants., Nagy T, Nurizzo D, Davies GJ, Biely P, Lakey JH, Bolam DN, Gilbert HJ, J Biol Chem. 2003 May 30;278(22):20286-92. Epub 2003 Mar 24. PMID:12654910
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