Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4OUI

Structure of Vibrio cholerae chitin de-N-acetylase in complex with TRIACETYLCHITOTRIOSE (CTO)

Summary for 4OUI
Entry DOI10.2210/pdb4oui/pdb
Related4NY2 4NYU 4NYY 4NZ1 4NZ3 4NZ4 4NZ5
Related PRD IDPRD_900017
DescriptorDeacetylase DA1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (6 entities in total)
Functional Keywords(beta/alpha)7, carbohydrate esterase, hydrolase
Biological sourceVibrio cholerae
Total number of polymer chains2
Total formula weight95536.78
Authors
Albesa-Jove, D.,Andres, E.,Biarnes, X.,Planas, A.,Guerin, M.E. (deposition date: 2014-02-17, release date: 2014-08-13, Last modification date: 2024-11-13)
Primary citationAndres, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.17 Å)
Structure validation

227933

PDB entries from 2024-11-27

PDB statisticsPDBj update infoContact PDBjnumon