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

Nat Commun. 2023 Feb 22;14(1):1001. doi: 10.1038/s41467-023-36604-y.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Adenosine Triphosphate / metabolism
  • Escherichia coli Proteins* / metabolism
  • Escherichia coli* / enzymology
  • Organophosphonates* / metabolism

Substances

  • Adenosine Triphosphatases
  • Adenosine Triphosphate
  • carbon-phosphorus lyase
  • Escherichia coli Proteins
  • Organophosphonates