Structure and Protein-Protein Interactions of Ice Nucleation Proteins Drive Their Activity.
atmospheric bacteria
ice-nucleating proteins
protein activity
protein structure
protein–protein interactions
Journal
Frontiers in microbiology
ISSN: 1664-302X
Titre abrégé: Front Microbiol
Pays: Switzerland
ID NLM: 101548977
Informations de publication
Date de publication:
2022
2022
Historique:
received:
09
02
2022
accepted:
16
05
2022
entrez:
5
7
2022
pubmed:
6
7
2022
medline:
6
7
2022
Statut:
epublish
Résumé
Microbially-produced ice nucleating proteins (INpro) are unique molecular structures with the highest known catalytic efficiency for ice formation. Airborne microorganisms utilize these proteins to enhance their survival by reducing their atmospheric residence times. INpro also have critical environmental effects including impacts on the atmospheric water cycle, through their role in cloud and precipitation formation, as well as frost damage on crops. INpro are ubiquitously present in the atmosphere where they are emitted from diverse terrestrial and marine environments. Even though bacterial genes encoding INpro have been discovered and sequenced decades ago, the details of how the INpro molecular structure and oligomerization foster their unique ice-nucleation activity remain elusive. Using machine-learning based software AlphaFold 2 and trRosetta, we obtained and analysed the first
Identifiants
pubmed: 35783412
doi: 10.3389/fmicb.2022.872306
pmc: PMC9247515
doi:
Types de publication
Journal Article
Langues
eng
Pagination
872306Informations de copyright
Copyright © 2022 Hartmann, Ling, Dreyer, Zipori, Finster, Grawe, Jensen, Borck, Reicher, Drace, Niedermeier, Jones, Hoffmann, Wex, Rudich, Boesen and Šantl-Temkiv.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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