Details

Autor(en) / Beteiligte

• Amstrup, Søren K
• Ong, Sui Ching
• Sofos, Nicholas
• Karlsen, Jesper L
• Skjerning, Ragnhild B
• Boesen, Thomas
• Enghild, Jan J
• Hove-Jensen, Bjarne
• Brodersen, Ditlev E

Titel

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

Ist Teil von

• Nature communications, 2023-02, Vol.14 (1), p.1001-1001, Article 1001

Ort / Verlag

England: Nature Publishing Group

Erscheinungsjahr

2023

Link zum Volltext

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• 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.