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.

Supported content

References

  1. Nature Communications 13, 5577 (2022). doi: 10.1038/s41467-022-33180-5
Institutions Authors Share
Autonomous University of Barcelona (UAB), Spain
3.000000
0.23
The University of Adelaide (Adelaide Uni), Australia
2.500000
0.19
University of Barcelona (UB), Spain
2.500000
0.19
Centre de Recherches sur les Macromolécules Végétales (CERMAV), France
2.000000
0.15
The University of Melbourne (UniMelb), Australia
1.000000
0.08
Suranaree University of Technology (SUT), Thailand
1.000000
0.08
Catalan Institution for Research and Advanced Studies (ICREA), Spain
0.500000
0.04
Huaiyin Normal University (HYTC), China
0.500000
0.04