Structural highlights
Function
PHNG_ECOLI Together with PhnH, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.[1]
Publication Abstract from PubMed
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.
Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase.,Amstrup SK, Ong SC, Sofos N, Karlsen JL, Skjerning RB, Boesen T, Enghild JJ, Hove-Jensen B, Brodersen DE Nat Commun. 2023 Feb 22;14(1):1001. doi: 10.1038/s41467-023-36604-y. PMID:36813778[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kamat SS, Williams HJ, Raushel FM. Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature. 2011 Nov 16;480(7378):570-3. doi: 10.1038/nature10622. PMID:22089136 doi:http://dx.doi.org/10.1038/nature10622
- ↑ Amstrup SK, Ong SC, Sofos N, Karlsen JL, Skjerning RB, Boesen T, Enghild JJ, Hove-Jensen B, Brodersen DE. Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase. Nat Commun. 2023 Feb 22;14(1):1001. PMID:36813778 doi:10.1038/s41467-023-36604-y
