2ac1
From Proteopedia
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Crystal structure of a cell-wall invertase from Arabidopsis thaliana
Overview
Cell-wall invertases play crucial roles during plant development. They, hydrolyse sucrose into its fructose and glucose subunits by cleavage of, the alpha1-beta2 glycosidic bond. Here, the structure of the Arabidopsis, thaliana cell-wall invertase 1 (AtcwINV1; gene accession code At3g13790), is described at a resolution of 2.15 A. The structure comprises an, N-terminal fivefold beta-propeller domain followed by a C-terminal domain, formed by two beta-sheets. The active site is positioned in the fivefold, beta-propeller domain, containing the nucleophile Asp23 and the acid/base, catalyst Glu203 of the double-displacement enzymatic reaction. The, function of the C-terminal domain remains unknown. Unlike in other GH 32, family enzyme structures known to date, in AtcwINV1 the cleft formed, between both domains is blocked by Asn299-linked carbohydrates. A, preliminary site-directed mutagenesis experiment (Asn299Asp) removed the, glycosyl chain but did not alter the activity profile of the enzyme.
About this Structure
2AC1 is a Single protein structure of sequence from Arabidopsis thaliana with and as ligands. Active as Beta-fructofuranosidase, with EC number 3.2.1.26 Full crystallographic information is available from OCA.
Reference
X-ray diffraction structure of a cell-wall invertase from Arabidopsis thaliana., Verhaest M, Lammens W, Le Roy K, De Coninck B, De Ranter CJ, Van Laere A, Van den Ende W, Rabijns A, Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1555-63. Epub 2006, Nov 23. PMID:17139091
Page seeded by OCA on Tue Jan 29 17:58:56 2008
