2ac1
Crystal structure of a cell-wall invertase from Arabidopsis thalianaCrystal structure of a cell-wall invertase from Arabidopsis thaliana
Structural highlights
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 PubMedCell-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||