The evolutionary advantage of an aromatic clamp in plant family 3 glycoside exo-hydrolases

Sukanya Luang, Xavier Fernández-Luengo, Alba Nin-Hill, Victor A. Streltsov, Julian G. Schwerdt, Santiago Alonso-Gil, James R. Ketudat Cairns, Stéphanie Pradeau, Sébastien Fort, Jean-Didier Maréchal, Laura Masgrau, Carme Rovira and Maria Hrmova ()
Additional contact information
Sukanya Luang: University of Adelaide, Waite Research Precinct
Xavier Fernández-Luengo: Universitat Autònoma de Barcelona
Alba Nin-Hill: Universitat de Barcelona
Victor A. Streltsov: University of Melbourne
Julian G. Schwerdt: University of Adelaide, Waite Research Precinct
Santiago Alonso-Gil: Universitat de Barcelona
James R. Ketudat Cairns: Suranaree University of Technology
Stéphanie Pradeau: Université Grenoble Alpes, Centre de Recherches sur les Macromolécules Végétales
Sébastien Fort: Université Grenoble Alpes, Centre de Recherches sur les Macromolécules Végétales
Jean-Didier Maréchal: Universitat Autònoma de Barcelona
Laura Masgrau: Universitat Autònoma de Barcelona
Carme Rovira: Universitat de Barcelona
Maria Hrmova: University of Adelaide, Waite Research Precinct

Nature Communications, 2022, vol. 13, issue 1, 1-19

Abstract: 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.

Date: 2022
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-022-33180-5 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-33180-5

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-022-33180-5

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().