2OXB
Crystal structure of a cell-wall invertase (E203Q) from Arabidopsis thaliana in complex with sucrose
2OXB の概要
エントリーDOI | 10.2210/pdb2oxb/pdb |
関連するPDBエントリー | 2AC1 |
関連するBIRD辞書のPRD_ID | PRD_900003 |
分子名称 | Beta-fructofuranosidase, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
機能のキーワード | hydrolase |
由来する生物種 | Arabidopsis thaliana (thale cress) |
細胞内の位置 | Secreted, extracellular space, apoplast (Probable): Q43866 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 62107.98 |
構造登録者 | Lammens, W.,Le Roy, K.,Van Laere, A.,Van den Ende, W.,Rabijns, A. (登録日: 2007-02-20, 公開日: 2008-01-22, 最終更新日: 2024-11-13) |
主引用文献 | Matrai, J.,Lammens, W.,Jonckheer, A.,Le Roy, K.,Rabijns, A.,Van den Ende, W.,De Maeyer, M. An alternate sucrose binding mode in the E203Q Arabidopsis invertase mutant: An X-ray crystallography and docking study. Proteins, 71:552-564, 2007 Cited by PubMed Abstract: In the present study, we report on the X-ray crystallographic structure of a GH32 invertase mutant, (i.e., the Arabidopsis thaliana cell-wall invertase 1-E203Q, AtcwINV1-mutant) in complex with sucrose. This structure was solved to reveal the features of sugar binding in the catalytic pocket. However, as demonstrated by the X-ray structure the sugar binding and the catalytic pocket arrangement is significantly altered as compared with what was expected based on previous X-ray structures on GH-J clan enzymes. We performed a series of docking and molecular dynamics simulations on various derivatives of AtcwINV1 to reveal the reasons behind this modified sugar binding. Our results demonstrate that the E203Q mutation introduced into the catalytic pocket triggers conformational changes that alter the wild type substrate binding. In addition, this study also reveals the putative productive sucrose binding modus in the wild type enzyme. PubMed: 17963237DOI: 10.1002/prot.21700 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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