2AC1

Crystal structure of a cell-wall invertase from Arabidopsis thaliana

2AC1 の概要

• エントリーDOI: 10.2210/pdb2ac1/pdb
• 分子名称: invertase, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[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, ... (6 entities in total)
• 機能のキーワード: five fold beta propeller, 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: 63722.53

構造登録者

Verhaest, M.,Le Roy, K.,De Ranter, C.,Van Laere, A.,Van den Ende, W.,Rabijns, A. (登録日: 2005-07-18, 公開日: 2006-08-29, 最終更新日: 2024-10-30)

主引用文献

Verhaest, M.,Lammens, W.,Le Roy, K.,De Coninck, B.,De Ranter, C.J.,Van Laere, A.,Van den Ende, W.,Rabijns, A.
X-ray diffraction structure of a cell-wall invertase from Arabidopsis thaliana.
Acta Crystallogr.,Sect.D, 62:1555-1563, 2006

PubMed Abstract: Cell-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.

PubMed: 17139091
DOI: 10.1107/S0907444906044489

実験手法

X-RAY DIFFRACTION (2.15 Å)