2QQW

Crystal structure of a cell-wall invertase (D23A) from Arabidopsis thaliana in complex with sucrose

2QQW の概要

• エントリーDOI: 10.2210/pdb2qqw/pdb
• 関連するPDBエントリー: 2AC1 2OXB 2QQV
• 関連するBIRD辞書のPRD_ID: PRD_900003
• 分子名称: Beta-fructofuranosidase, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]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, ... (7 entities in total)
• 機能のキーワード: hydrolase, invertase, glycosidase
• 由来する生物種: Arabidopsis thaliana (thale cress)
• 細胞内の位置: Secreted, extracellular space, apoplast : Q43866
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 63381.53

構造登録者

Lammens, W.,Le Roy, K.,Van Laere, A.,Rabijns, A.,Van den Ende, W. (登録日: 2007-07-27, 公開日: 2008-04-22, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.8 Å)