The evolutionary advantage of an aromatic clamp in plant family 3 glycoside exo-hydrolases
- Journal:
- Nature Communications
- Published:
- DOI:
- 10.1038/s41467-022-33180-5
- Affiliations:
- 9
- Authors:
- 13
Research Highlight
Discovering the dynamics of a barley enzyme
© sot/Stone/Getty Images
An analysis of how an important plant enzyme changes shape during binding could help researchers to improve cereal production.
Enzymes known as glycoside hydrolase family 3 (GH3) are found in bacteria, fungi and many plants, including crop plants. Nearly 50,000 have been categorized so far, but only the one found in the cereal barley has had its atomic structure determined. However, even for this enzyme, very little is known how its structure changes when it interacts with other molecules.
Now, a team led by researchers from the University of Adelaide in Australia has shown how the enzyme flexes when sugars in it bind.
In addition to potentially enhancing barley yields, this information could also help develop enzymes that can be used in chemical and medical applications, the researchers say.
References
- Nature Communications 13, 5577 (2022). doi: 10.1038/s41467-022-33180-5