7Z15

E. coli C-P lyase bound to a PhnK/PhnL dual ABC dimer and ADP + Pi

Summary for 7Z15

• Entry DOI: 10.2210/pdb7z15/pdb
• EMDB information: 14441
• Descriptor: Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG, PHOSPHATE ION, MAGNESIUM ION, ... (13 entities in total)
• Functional Keywords: protein complex, transferase, abc, hydrolase, lyase, carbon phosphorus
• Biological source: Escherichia coli; More
• Total number of polymer chains: 12
• Total formula weight: 333342.38

Authors

Amstrup, S.K.,Sofos, N.,Karlsen, J.L.,Skjerning, R.B.,Boesen, T.,Enghild, J.J.,Hove-Jensen, B.,Brodersen, D.E. (deposition date: 2022-02-24, release date: 2022-06-22, Last modification date: 2024-07-17)

Primary citation

Amstrup, S.K.,Ong, S.C.,Sofos, N.,Karlsen, J.L.,Skjerning, R.B.,Boesen, T.,Enghild, J.J.,Hove-Jensen, B.,Brodersen, D.E.
Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase.
Nat Commun, 14:1001-1001, 2023

PubMed 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.

PubMed: 36813778
DOI: 10.1038/s41467-023-36604-y

Experimental method

ELECTRON MICROSCOPY (1.93 Å)