2QQU

Crystal structure of a cell-wall invertase (D239A) from Arabidopsis thaliana in complex with sucrose

Summary for 2QQU

• Entry DOI: 10.2210/pdb2qqu/pdb
• Related: 2AC1 2OXB
• Related PRD ID: PRD_900003
• Descriptor: Beta-fructofuranosidase, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: hydrolase, invertase, glycosidase
• Biological source: Arabidopsis thaliana (thale cress)
• Cellular location: Secreted, extracellular space, apoplast (Probable): Q43866
• Total number of polymer chains: 1
• Total formula weight: 63204.29

Authors

Lammens, W.,Le Roy, K.,Van Laere, A.,Rabijns, A.,Van den Ende, W. (deposition date: 2007-07-27, release date: 2008-04-22, Last modification date: 2023-08-30)

Primary citation

Lammens, W.,Le Roy, K.,Van Laere, A.,Rabijns, A.,Van den Ende, W.
Crystal structures of Arabidopsis thaliana cell-wall invertase mutants in complex with sucrose.
J.Mol.Biol., 377:378-385, 2008

PubMed Abstract: In 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.

PubMed: 18258263
DOI: 10.1016/j.jmb.2007.12.074

Experimental method

X-RAY DIFFRACTION (2.84 Å)