ArticleNature communications2022
The evolutionary advantage of an aromatic clamp in plant family 3 glycoside exo-hydrolases.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Crystal structure ofProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Understanding Biases in Liquid-Liquid Phase Separation: Investigating Amino Acid Enrichments in Phase-Separating Proteins toward Peptide Design.Biomacromolecules · 2025Article
- Report of the 5th International Symposium on Frontiers in Molecular Science (ISFMS 2025).International journal of molecular sciences · 2025Article
- The structure and dynamics of water molecule networks underlie catalytic efficiency in a glycoside exo-hydrolase.Communications biology · 2025Article
- Enzymes in 3D: Synthesis, remodelling, and hydrolysis of cell wall (1,3;1,4)-β-glucans.Plant physiology · 2023Article
- Molecular mechanisms of processive glycoside hydrolases underline catalytic pragmatism.Biochemical Society transactions · 2023Article
- The evolutionary advantage of an aromatic clamp in plant family 3 glycoside exo-hydrolases.Nature communications · 2022Article
Corrections and comments
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Authors and funding
13 authors at 8 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the barley β-D-glucan glucohydrolase, a glycoside hydrolase family 3 (GH3) enzyme, the Trp286/Trp434 clamp ensures β-D-glucosides binding, which is fundamental for substrate hydrolysis during plant growth and development. We employ mutagenesis, high-resolution X-ray crystallography, and multi-scale molecular modelling methods to examine the binding and conformational behaviour of isomeric β-D-glucosides during substrate-product assisted processive catalysis that operates in GH3 hydrolases. Enzyme kinetics reveals that the W434H mutant retains broad specificity, while W434A behaves as a strict (1,3)-β-D-glucosidase. Investigations of reactant movements on the nanoscale reveal that processivity is sensitive to mutation-specific alterations of the tryptophan clamp. While wild-type and W434H utilise a lateral cavity for glucose displacement and sliding of (1,3)-linked hydrolytic products through the catalytic site without dissociation, consistent with their high hydrolytic rates, W434A does not adopt processive catalysis. Phylogenomic analyses of GH3 hydrolases disclose the evolutionary advantage of the tryptophan clamp that confers broad specificity, high catalytic efficiency, and processivity.
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