2IW0

Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum

2IW0 の概要

• エントリーDOI: 10.2210/pdb2iw0/pdb
• 分子名称: CHITIN DEACETYLASE, ZINC ION, ACETATE ION, ... (6 entities in total)
• 機能のキーワード: hydrolase, chitin de-n-acetylase, family 4 carbohydrate esterase
• 由来する生物種: COLLETOTRICHUM LINDEMUTHIANUM (GLOMERELLA LINDEMUTHIANA)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28277.01

構造登録者

Blair, D.E.,Hekmat, O.,Schuttelkopf, A.W.,Shrestha, B.,Tokuyasu, K.,Withers, S.G.,van Aalten, D.M.F. (登録日: 2006-06-23, 公開日: 2006-07-04, 最終更新日: 2024-10-09)

主引用文献

Blair, D.E.,Hekmat, O.,Schuttelkopf, A.W.,Shrestha, B.,Tokuyasu, K.,Withers, S.G.,Van Aalten, D.M.F.
Structure and Mechanism of Chitin Deacetylase from the Fungal Pathogen Colletotrichum Lindemuthianum.
Biochemistry, 45:9416-, 2006

PubMed Abstract: The fungal pathogen Colletotrichum lindemuthianum secretes an endo-chitin de-N-acetylase (ClCDA) to modify exposed hyphal chitin during penetration and infection of plants. Although a significant amount of biochemical data is available on fungal chitin de-N-acetylases, no structural data exist. Here we describe the 1.8 A crystal structure of a ClCDA product complex and the analysis of the reaction mechanism using Hammett linear free energy relationships, subsite probing, and atomic absorption spectroscopy studies. The structural data in combination with biochemical data reveal that ClCDA consists of a single domain encompassing a mononuclear metalloenzyme which employs a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. The data presented here indicate that ClCDA possesses a highly conserved substrate-binding groove, with subtle alterations that influence substrate specificity and subsite affinity. Strikingly, the structure also shows that the hexahistidine purification tag appears to form a tight interaction with the active site groove. The enzyme requires occupancy of at least the 0 and +1 subsites by (GlcNAc)(2) for activity and proceeds through a tetrahedral oxyanion intermediate.

PubMed: 16878976
DOI: 10.1021/BI0606694

実験手法

X-RAY DIFFRACTION (1.81 Å)