ArticleActa crystallographica. Section D, Biological crystallography2014
Structural characteristics of an insect group I chitinase, an enzyme indispensable to moulting.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 75 citations in OpenAlex.
- Functional Characterization and Antifungal Activity of Insect-Derived Chitinases Expressed inPolymers · 2026Article
- Virtual screening of a random tripeptide library for easily prepared inhibitors of insect chitinolytic enzymes.Cell surface (Amsterdam, Netherlands) · 2025Article
- Molecular identification of the chitinase genes in Aedes albopictus and essential roles of AaCht10 in pupal-adult transition.Parasites & vectors · 2023Article
- Pan-Genomes Provide Insights into the Genetic Basis ofJournal of fungi (Basel, Switzerland) · 2022Article
- GH18 endo-β-N-acetylglucosaminidases use distinct mechanisms to process hybrid-type N-linked glycans.The Journal of biological chemistry · 2021Article
- Molecular Basis of Broad SpectrumACS central science · 2019Article
- Chitinase: diversity, limitations, and trends in engineering for suitable applications.Bioscience reports · 2018Review
- Structural analysis of group II chitinase (ChtII) catalysis completes the puzzle of chitin hydrolysis in insects.The Journal of biological chemistry · 2018Article
- The deduced role of a chitinase containing two nonsynergistic catalytic domains.Acta crystallographica. Section D, Structural biology · 2018Article
- Structure, Catalysis, and Inhibition ofThe Journal of biological chemistry · 2017Article
- Inverse relationship between chitobiase and transglycosylation activities of chitinase-D from Serratia proteamaculans revealed by mutational and biophysical analyses.Scientific reports · 2015Article
- Fully deacetylated chitooligosaccharides act as efficient glycoside hydrolase family 18 chitinase inhibitors.The Journal of biological chemistry · 2014Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Insects possess a greater number of chitinases than any other organisms. This work is the first report of unliganded and oligosaccharide-complexed crystal structures of the insect chitinase OfChtI from Ostrinia furnacalis, which is essential to moulting. The obtained crystal structures were solved at resolutions between 1.7 and 2.2 Å. A structural comparison with other chitinases revealed that OfChtI contains a long substrate-binding cleft similar to the bacterial chitinase SmChiB from Serratia marcescens. However, unlike the exo-acting SmChiB, which has a blocked and tunnel-like cleft, OfChtI possesses an open and groove-like cleft. The complexed structure of the catalytic domain of OfChtI (OfChtI-CAD) with (GlcNAc)2/3 indicates that the reducing sugar at subsite -1 is in an energetically unfavoured `boat' conformation, a state that possibly exists just before the completion of catalysis. Because OfChtI is known to act from nonreducing ends, (GlcNAc)3 would be a hydrolysis product of (GlcNAc)6, suggesting that OfChtI possesses an endo enzymatic activity. Furthermore, a hydrophobic plane composed of four surface-exposed aromatic residues is adjacent to the entrance to the substrate-binding cleft. Mutations of these residues greatly impair the chitin-binding activity, indicating that this hydrophobic plane endows OfChtI-CAD with the ability to anchor chitin. This work reveals the unique structural characteristics of an insect chitinase.
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