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, Ditlev E Brodersen

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10 Citations (Scopus)

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.

Original languageEnglish
Article number1001
JournalNature Communications
Volume14
ISSN2041-1723
DOIs
Publication statusPublished - Feb 2023

Keywords

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

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