4NYU

Structure of Vibrio cholerae chitin de-N-acetylase in complex with acetate ion (ACT) in C 2 2 21

4NYU の概要

• エントリーDOI: 10.2210/pdb4nyu/pdb
• 関連するPDBエントリー: 4NY2 4NYY 4NZ1 4NZ3 4NZ4 4NZ5
• 分子名称: Deacetylase DA1, ZINC ION, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: (beta/alpha)7, carbohydrate esterase, hydrolase
• 由来する生物種: Vibrio cholerae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47917.30

構造登録者

Albesa-Jove, D.,Andres, E.,Biarnes, X.,Planas, A.,Guerin, M.E. (登録日: 2013-12-11, 公開日: 2014-08-13, 最終更新日: 2024-10-16)

主引用文献

Andres, E.,Albesa-Jove, D.,Biarnes, X.,Moerschbacher, B.M.,Guerin, M.E.,Planas, A.
Structural basis of chitin oligosaccharide deacetylation.
Angew.Chem.Int.Ed.Engl., 53:6882-6887, 2014

PubMed Abstract: Cell signaling and other biological activities of chitooligosaccharides (COSs) seem to be dependent not only on the degree of polymerization, but markedly on the specific de-N-acetylation pattern. Chitin de-N-acetylases (CDAs) catalyze the hydrolysis of the acetamido group in GlcNAc residues of chitin, chitosan, and COS. A major challenge is to understand how CDAs specifically define the distribution of GlcNAc and GlcNH2 moieties in the oligomeric chain. We report the crystal structure of the Vibrio cholerae CDA in four relevant states of its catalytic cycle. The two enzyme complexes with chitobiose and chitotriose represent the first 3D structures of a CDA with its natural substrates in a productive mode for catalysis, thereby unraveling an induced-fit mechanism with a significant conformational change of a loop closing the active site. We propose that the deacetylation pattern exhibited by different CDAs is governed by critical loops that shape and differentially block accessible subsites in the binding cleft of CE4 enzymes.

PubMed: 24810719
DOI: 10.1002/anie.201400220

実験手法

X-RAY DIFFRACTION (2.03 Å)