ArticleNature communications2024
Remote loop evolution reveals a complex biological function for chitinase enzymes beyond the active site.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- The glycosylated root-knot nematode effector Minc10750 suppresses plant immunity by destabilizing host chitinases.The New phytologist · 2026Article
- Conserved protein folds underpin the diversification of secreted proteins in a fungal pathogen.BMC microbiology · 2026Article
- Domain gain or loss in a fungal chitinase enables specialization towards antagonism or immune suppression.Nature communications · 2026Article
- Characterization of an Atypical GH19 Family Chitinase fromMicroorganisms · 2026Article
- Green bioconversion of insoluble chitin: chitinase development pathways via multi-strategy synergy.Bioresources and bioprocessing · 2026Review
- Conformational Dynamics and Catalytic Backups in a Hyper-thermostable Engineered Archaeal Protein Tyrosine Phosphatase.JACS Au · 2026Article
- Microbial chitinases in the plant holobiont: ecological roles and structural determinants.FEMS microbiology reviews · 2026Review
- A scalable equivariant graph network framework for precise protein function prediction.Genome biology · 2025Article
- Fine mapping, introgression, and KASP marker development for powdery mildew resistance in watermelon using an interspecific RIL population (Citrullus mucosospermus × C. lanatus).TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025Article
- Genome-Wide Identification and Expression Analysis of the GH19 Chitinase Gene Family in Sea Island Cotton.Current issues in molecular biology · 2025Article
- Expression of endochitinase and exochitinase in lettuce chloroplasts increases plant biomass and kills fungal pathogen Candida albicans.Plant biotechnology journal · 2025Article
- From duplication to fusion: Expanding Dayhoff's model of protein evolution.Protein science : a publication of the Protein Society · 2025Review
Corrections and comments
- Erratum issued
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Loops are small secondary structural elements that play a crucial role in the emergence of new enzyme functions. However, the evolutionary molecular mechanisms how proteins acquire these loop elements and obtain new function is poorly understood. To address this question, we study glycoside hydrolase family 19 (GH19) chitinase-an essential enzyme family for pathogen degradation in plants. By revealing the evolutionary history and loops appearance of GH19 chitinase, we discover that one loop which is remote from the catalytic site, is necessary to acquire the new antifungal activity. We demonstrate that this remote loop directly accesses the fungal cell wall, and surprisingly, it needs to adopt a defined structure supported by long-range intramolecular interactions to perform its function. Our findings prove that nature applies this strategy at the molecular level to achieve a complex biological function while maintaining the original activity in the catalytic pocket, suggesting an alternative way to design new enzyme function.
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