Design and characterization of a protein fold switching network.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
26 01 2023
26 01 2023
Historique:
received:
14
07
2022
accepted:
13
01
2023
entrez:
26
1
2023
pubmed:
27
1
2023
medline:
31
1
2023
Statut:
epublish
Résumé
To better understand how amino acid sequence encodes protein structure, we engineered mutational pathways that connect three common folds (3α, β-grasp, and α/β-plait). The structures of proteins at high sequence-identity intersections in the pathways (nodes) were determined using NMR spectroscopy and analyzed for stability and function. To generate nodes, the amino acid sequence encoding a smaller fold is embedded in the structure of an ~50% larger fold and a new sequence compatible with two sets of native interactions is designed. This generates protein pairs with a 3α or β-grasp fold in the smaller form but an α/β-plait fold in the larger form. Further, embedding smaller antagonistic folds creates critical states in the larger folds such that single amino acid substitutions can switch both their fold and function. The results help explain the underlying ambiguity in the protein folding code and show that new protein structures can evolve via abrupt fold switching.
Identifiants
pubmed: 36702827
doi: 10.1038/s41467-023-36065-3
pii: 10.1038/s41467-023-36065-3
pmc: PMC9879998
doi:
Substances chimiques
Proteins
0
Staphylococcal Protein A
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
431Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM062154
Pays : United States
Organisme : NIGMS NIH HHS
ID : R44 GM126676
Pays : United States
Informations de copyright
© 2023. The Author(s).
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