7z17

E. coli C-P lyase bound to a PhnK ABC dimer in an open conformation

spinqualitylabelsall models 7z17, resolution 2.57Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7z17 is a 10 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.57Å Ligands: I9X, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PHNK_ECOLI Belongs to an operon involved in alkylphosphonate uptake and C-P lyase. Exact function not known. PhnK is not required for the ribophosphonate triphosphate (RPnTP) synthase reaction. Publication Abstract from PubMed 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. Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase.,Amstrup SK, Ong SC, Sofos N, Karlsen JL, Skjerning RB, Boesen T, Enghild JJ, Hove-Jensen B, Brodersen DE Nat Commun. 2023 Feb 22;14(1):1001. doi: 10.1038/s41467-023-36604-y. PMID:36813778 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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