Design of allosteric sites into rotary motor V
Journal
Nature chemistry
ISSN: 1755-4349
Titre abrégé: Nat Chem
Pays: England
ID NLM: 101499734
Informations de publication
Date de publication:
Nov 2023
Nov 2023
Historique:
received:
11
05
2021
accepted:
26
05
2023
medline:
6
11
2023
pubmed:
7
7
2023
entrez:
6
7
2023
Statut:
ppublish
Résumé
Allostery produces concerted functions of protein complexes by orchestrating the cooperative work between the constituent subunits. Here we describe an approach to create artificial allosteric sites in protein complexes. Certain protein complexes contain subunits with pseudo-active sites, which are believed to have lost functions during evolution. Our hypothesis is that allosteric sites in such protein complexes can be created by restoring the lost functions of pseudo-active sites. We used computational design to restore the lost ATP-binding ability of the pseudo-active site in the B subunit of a rotary molecular motor, V
Identifiants
pubmed: 37414880
doi: 10.1038/s41557-023-01256-4
pii: 10.1038/s41557-023-01256-4
pmc: PMC10624635
doi:
Substances chimiques
Vacuolar Proton-Translocating ATPases
EC 3.6.1.-
Adenosine Triphosphate
8L70Q75FXE
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1591-1598Subventions
Organisme : MEXT | Japan Society for the Promotion of Science (JSPS)
ID : 18H05420
Organisme : MEXT | Japan Society for the Promotion of Science (JSPS)
ID : 18H05424
Organisme : MEXT | JST | Precursory Research for Embryonic Science and Technology (PRESTO)
ID : JPMJPR20E6
Organisme : MEXT | JST | Precursory Research for Embryonic Science and Technology (PRESTO)
ID : JPMJPR13AD
Organisme : Japan Agency for Medical Research and Development (AMED)
ID : BINDS0471
Informations de copyright
© 2023. The Author(s).
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