Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
22 02 2023
22 02 2023
Historique:
received:
03
05
2022
accepted:
08
02
2023
entrez:
22
2
2023
pubmed:
23
2
2023
medline:
25
2
2023
Statut:
epublish
Résumé
In Escherichia coli, the 14-cistron phn operon encoding carbon-phosphorus lyase allows for utilisation of phosphorus from a wide range of stable phosphonate compounds containing a C-P bond. As part of a complex, multi-step pathway, the PhnJ subunit was shown to cleave the C-P bond via a radical mechanism, however, the details of the reaction could not immediately be reconciled with the crystal structure of a 220 kDa PhnGHIJ C-P lyase core complex, leaving a significant gap in our understanding of phosphonate breakdown in bacteria. Here, we show using single-particle cryogenic electron microscopy that PhnJ mediates binding of a double dimer of the ATP-binding cassette proteins, PhnK and PhnL, to the core complex. ATP hydrolysis induces drastic structural remodelling leading to opening of the core complex and reconfiguration of a metal-binding and putative active site located at the interface between the PhnI and PhnJ subunits.
Identifiants
pubmed: 36813778
doi: 10.1038/s41467-023-36604-y
pii: 10.1038/s41467-023-36604-y
pmc: PMC9947105
doi:
Substances chimiques
Adenosine Triphosphatases
EC 3.6.1.-
Adenosine Triphosphate
8L70Q75FXE
carbon-phosphorus lyase
EC 4.99.-
Escherichia coli Proteins
0
Organophosphonates
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1001Informations de copyright
© 2023. The Author(s).
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