2gh4
From Proteopedia
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YteR/D143N/dGalA-Rha
Overview
Bacillus subtilis strain 168 YteR has been identified as a novel enzyme, "unsaturated rhamnogalacturonyl hydrolase" classified in glycoside, hydrolase family 105. This enzyme acts specifically on unsaturated, rhamnogalacturonan (RG) produced from plant cell wall RG type-I treated, with RG lyases, releasing unsaturated galacturonic acid (DeltaGalA) from, the substrate. The most likely candidate catalytic residue is Asp-143., Here, we show the structure of D143N in complex with unsaturated RG, disaccharide (substrate) determined at 1.9A resolution by X-ray, crystallography. This structural feature directly contributes to the, postulation of the enzyme reaction mechanism. YteR triggers the hydration, of vinyl ether group in DeltaGalA, but not of glycoside bond, by using, Asp-143 as a general acid and base catalyst. Asp-143 donates proton to the, double bond of DeltaGalA as an acid catalyst and also deprotonates a water, molecule as a base catalyst. Deprotonated water molecule attacks the C5, atom of DeltaGalA.
About this Structure
2GH4 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Structure of unsaturated rhamnogalacturonyl hydrolase complexed with substrate., Itoh T, Ochiai A, Mikami B, Hashimoto W, Murata K, Biochem Biophys Res Commun. 2006 Sep 8;347(4):1021-9. Epub 2006 Jul 17. PMID:16870154
Page seeded by OCA on Wed Nov 21 11:12:08 2007
