Structural remodelling of the carbon–phosphorus lyase machinery by a dual ABC ATPase
Søren Kirk Amstrup, Sui Ching Ong, Nicholas Sofos, Jesper Lykkegaard Karlsen, Ragnhild Bager Skjerning, Thomas Boesen, Jan J. Enghild, Bjarne Hove‐Jensen, Ditlev E. Brodersen
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.