ArticlePlant molecular biology2011
Crystal structure and mode of action of a class V chitinase from Nicotiana tabacum.
Article in Plant molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 54 citations in OpenAlex.
- Chitinase-activity-independent anti-insect effect of class V chitinase from fig trees (Ficus carica).Planta · 2025Article
- Cis-nonProline peptides: Genuine occurrences and their functional roles.Protein science : a publication of the Protein Society · 2025Article
- Enhancing the endo-activity of the thermophilic chitinase to yield chitooligosaccharides with high degrees of polymerization.Bioresources and bioprocessing · 2024Article
- AlphaFold-Multimer predicts cross-kingdom interactions at the plant-pathogen interface.Nature communications · 2023Article
- Genome-Wide Identification and Expression of Chitinase Class I Genes in Garlic (Plants (Basel, Switzerland) · 2021Article
- Thermophilic Chitinases: Structural, Functional and Engineering Attributes for Industrial Applications.Applied biochemistry and biotechnology · 2021Review
- Chitinase: diversity, limitations, and trends in engineering for suitable applications.Bioscience reports · 2018Review
- 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
- A single amino acid substitution in a chitinase of the legume Medicago truncatula is sufficient to gain Nod-factor hydrolase activity.Open biology · 2016Article
- Article
- Structural characteristics of an insect group I chitinase, an enzyme indispensable to moulting.Acta crystallographica. Section D, Biological crystallography · 2014Article
- The PDB database is a rich source of alpha-helical anti-microbial peptides to combat disease causing pathogens.F1000Research · 2014Article
- The nodulation factor hydrolase of Medicago truncatula: characterization of an enzyme specifically cleaving rhizobial nodulation signals.Plant physiology · 2013Article
- A class V chitinase from Arabidopsis thaliana: gene responses, enzymatic properties, and crystallographic analysis.Planta · 2011Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A class V chitinase from Nicotiana tabacum (NtChiV) with amino acid sequence similar to that of Serratia marcescens chitinase B (SmChiB) was expressed in E. coli and purified to homogeneity. When N-acetylglucosamine oligosaccharides [(NAG)(n)] were hydrolyzed by the purified NtChiV, the second glycosidic linkage from the non-reducing end was predominantly hydrolyzed in a manner similar to that of SmChiB. NtChiV was shown to hydrolyze partially N-acetylated chitosan non-processively, whereas SmChiB hydrolyzes the same substrate processively. The crystal structure of NtChiV was determined by the single-wavelength anomalous dispersion method at 1.2 Å resolution. The protein adopts a classical (β/α)₈-barrel fold (residues 1-233 and 303-348) with an insertion of a small (α + β) domain (residues 234-302). This is the first crystal structure of a plant class V chitinase. The crystal structure of the inactive mutant NtChiV E115Q complexed with (NAG)₄ was also solved and exhibited a linear conformation of the bound oligosaccharide occupying -2, +1, +2, and +3 subsites. The complex structure corresponds to an initial state of (NAG)₄ binding, which is proposed to be converted into a bent conformation through sliding of the +1, +2, and +3 sugar units to -1, +1, and +2 subsites. Although NtChiV is similar to SmChiB, the chitin-binding domain is present in the C-terminus of the latter, but not in the former. Aromatic amino acid residues found in the substrate binding cleft of SmChiB, including Trp97, are substituted with aliphatic residues in NtChiV. These structural differences appear to be responsible for NtChiV being a non-processive enzyme.
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