2qqv | pdb_00002qqv
Crystal structure of a cell-wall invertase (E203A) from Arabidopsis thaliana in complex with sucrose
Structural highlights
FunctionINV1_ARATH Beta-fructofuranosidase that can use sucrose and 1-kestose, and, to a lower extent, neokestose and levan, as substrates, but not inuline.[1] [2] 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 PubMedIn plants, cell-wall invertases fulfil important roles in carbohydrate partitioning, growth, development and crop yield. In this study, we report on different X-ray crystal structures of Arabidopsis thaliana cell-wall invertase 1 (AtcwINV1) mutants with sucrose. These structures reveal a detailed view of sucrose binding in the active site of the wild-type AtcwINV1. Compared to related enzyme-sucrose complexes, important differences in the orientation of the glucose subunit could be observed. The structure of the E203Q AtcwINV1 mutant showed a complete new binding modus, whereas the D23A, E203A and D239A structures most likely represent the productive binding modus. Together with a hydrophobic zone formed by the conserved W20, W47 and W82, the residues N22, D23, R148, E203, D149 and D239 are necessary to create the ideal sucrose-binding pocket. D239 can interact directly with the glucose moiety of sucrose, whereas K242 has an indirect role in substrate stabilization. Most probably, K242 keeps D239 in a favourable position upon substrate binding. Unravelling the exact position of sucrose in plant cell-wall invertases is a necessary step towards the rational design of superior invertases to further increase crop yield and biomass production. Crystal structures of Arabidopsis thaliana cell-wall invertase mutants in complex with sucrose.,Lammens W, Le Roy K, Van Laere A, Rabijns A, Van den Ende W J Mol Biol. 2008 Mar 21;377(2):378-85. Epub 2008 Jan 5. PMID:18258263[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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