Structural remodelling of the carbon–phosphorus lyase machinery by a dual ABC ATPase

Søren K. Amstrup, Sui Ching Ong, Nicholas Sofos, Jesper L. Karlsen, Ragnhild B. Skjerning, Thomas Boesen, Jan J. Enghild, Bjarne Hove-Jensen and Ditlev E. Brodersen ()
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Søren K. Amstrup: Aarhus University
Sui Ching Ong: Aarhus University
Nicholas Sofos: Aarhus University
Jesper L. Karlsen: Aarhus University
Ragnhild B. Skjerning: Aarhus University
Thomas Boesen: Interdisciplinary Nanoscience Centre (iNANO) Aarhus University
Jan J. Enghild: Aarhus University
Bjarne Hove-Jensen: Aarhus University
Ditlev E. Brodersen: Aarhus University

Nature Communications, 2023, vol. 14, issue 1, 1-12

Abstract: Abstract 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.

Date: 2023
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DOI: 10.1038/s41467-023-36604-y

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