ArticlePlant molecular biology2009
The first crystal structures of a family 19 class IV chitinase: the enzyme from Norway spruce.
Article in Plant molecular biology, 2009. 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, 56 citations in OpenAlex.
- Shotgun proteomics of quinoa seeds reveals chitinases enrichment under rainfed conditions.Scientific reports · 2023Article
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- Multi-functionality of a tryptophan residue conserved in substrate-binding groove of GH19 chitinases.Scientific reports · 2021Article
- The GH19 Engineering Database: Sequence diversity, substrate scope, and evolution in glycoside hydrolase family 19.PloS one · 2021Article
- Thermophilic Chitinases: Structural, Functional and Engineering Attributes for Industrial Applications.Applied biochemistry and biotechnology · 2021Review
- In Silico Characterization of a Unique Plant-Like "Loopful" GH19 Chitinase from Newly Isolated Chitinophaga sp. YS-16.Current microbiology · 2020Article
- Chitinase: diversity, limitations, and trends in engineering for suitable applications.Bioscience reports · 2018Review
- The Capsicum annuum class IV chitinase ChitIV interacts with receptor-like cytoplasmic protein kinase PIK1 to accelerate PIK1-triggered cell death and defence responses.Journal of experimental botany · 2015Article
- Crystallographic structure of ChitA, a glycoside hydrolase family 19, plant class IV chitinase from Zea mays.Protein science : a publication of the Protein Society · 2014Article
- Structural characteristics of an insect group I chitinase, an enzyme indispensable to moulting.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Article
- Crystallization and preliminary X-ray diffraction analysis of an active-site mutant of `loopless' family GH19 chitinase from Bryum coronatum in a complex with chitotetraose.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Truncation of class IV chitinases from Arabidopsis by secreted fungal proteases.Molecular plant pathology · 2012Article
- A comparative proteomic approach to analyse structure, function and evolution of rice chitinases: a step towards increasing plant fungal resistance.Journal of molecular modeling · 2012Article
- Crystallization and preliminary X-ray diffraction analysis of a class V chitinase from Nicotiana tabacum.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chitinases help plants defend themselves against fungal attack, and play roles in other processes, including development. The catalytic modules of most plant chitinases belong to glycoside hydrolase family 19. We report here x-ray structures of such a module from a Norway spruce enzyme, the first for any family 19 class IV chitinase. The bi-lobed structure has a wide cleft lined by conserved residues; the most interesting for catalysis are Glu113, the proton donor, and Glu122, believed to be a general base that activate a catalytic water molecule. Comparisons to class I and II enzymes show that loop deletions in the class IV proteins make the catalytic cleft shorter and wider; from modeling studies, it is predicted that only three N-acetylglucosamine-binding subsites exist in class IV. Further, the structural comparisons suggest that the family 19 enzymes become more closed on substrate binding. Attempts to solve the structure of the complete protein including the associated chitin-binding module failed, however, modeling studies based on close relatives indicate that the binding module recognizes at most three N-acetylglucosamine units. The combined results suggest that the class IV enzymes are optimized for shorter substrates than the class I and II enzymes, or alternatively, that they are better suited for action on substrates where only small regions of chitin chain are accessible. Intact spruce chitinase is shown to possess antifungal activity, which requires the binding module; removing this module had no effect on measured chitinase activity.
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