4OUI
Structure of Vibrio cholerae chitin de-N-acetylase in complex with TRIACETYLCHITOTRIOSE (CTO)
Summary for 4OUI
Entry DOI | 10.2210/pdb4oui/pdb |
Related | 4NY2 4NYU 4NYY 4NZ1 4NZ3 4NZ4 4NZ5 |
Related PRD ID | PRD_900017 |
Descriptor | Deacetylase 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 source | Vibrio cholerae |
Total number of polymer chains | 2 |
Total formula weight | 95536.78 |
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: 2023-11-08) |
Primary citation | 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 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: 24810719DOI: 10.1002/anie.201400220 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.17 Å) |
Structure validation
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