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7VI8

Crystal structure of ChbG

Summary for 7VI8
Entry DOI10.2210/pdb7vi8/pdb
DescriptorChitooligosaccharide deacetylase, ZINC ION, ACETATE ION, ... (4 entities in total)
Functional Keywordschbg, chitin catabolism, chitin deacetylase, chitobiose operon, klebsiella pneumoniae, hydrolase
Biological sourceKlebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
Total number of polymer chains2
Total formula weight56109.02
Authors
Lee, S.Y.,Park, H.H. (deposition date: 2021-09-26, release date: 2022-09-07, Last modification date: 2023-11-29)
Primary citationLee, S.Y.,Pardhe, B.D.,Oh, T.J.,Park, H.H.
Crystal structure of ChbG from Klebsiella pneumoniae reveals the molecular basis of diacetylchitobiose deacetylation.
Commun Biol, 5:862-862, 2022
Cited by
PubMed Abstract: The chitobiose (chb) operon is involved in the synthesis of chitooligosaccharide and is comprised of a BCARFG gene cluster. ChbG encodes a chitooligosaccharide deacetylase (CDA) which catalyzes the removal of one acetyl group from N,N'-diacetylchitobiose. It is considered a novel type of CDA due to its lack of sequence homology. Although there are various structural studies of CDAs linked to the kinetic properties of the enzyme, the structural information of ChbG is unavailable. In this study, the crystal structure of ChbG from Klebsiella pneumoniae is provided. The molecular basis of deacetylation of diacetylchitobiose by ChbG is determined based on structural analysis, mutagenesis, biophysical analysis, and in silico docking of the substrate, diacetylchitobiose. This study contributes towards a deeper understanding of chitin and chitosan biology, as well as provides a platform to engineer CDA biocatalysts.
PubMed: 36002585
DOI: 10.1038/s42003-022-03824-9
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.83 Å)
Structure validation

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