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

doi:10.1038/s41467-023-36604-y

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

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

7 Citationer (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.

Originalsprog	Engelsk
Artikelnummer	1001
Tidsskrift	Nature Communications
Vol/bind	14
ISSN	2041-1723
DOI	https://doi.org/10.1038/s41467-023-36604-y
Status	Udgivet - feb. 2023

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10.1038/s41467-023-36604-yLicens: CC BY

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title = "Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase",

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.",

keywords = "Adenosine Triphosphatases/metabolism, Adenosine Triphosphate/metabolism, Escherichia coli/enzymology, Escherichia coli Proteins/metabolism, Organophosphonates/metabolism",

author = "Amstrup, {S{\o}ren K} and Ong, {Sui Ching} and Nicholas Sofos and Karlsen, {Jesper L} and Skjerning, {Ragnhild B} and Thomas Boesen and Enghild, {Jan J} and Bjarne Hove-Jensen and Brodersen, {Ditlev E}",

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doi = "10.1038/s41467-023-36604-y",

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TY - JOUR

T1 - Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase

AU - Amstrup, Søren K

AU - Ong, Sui Ching

AU - Sofos, Nicholas

AU - Karlsen, Jesper L

AU - Skjerning, Ragnhild B

AU - Boesen, Thomas

AU - Enghild, Jan J

AU - Hove-Jensen, Bjarne

AU - Brodersen, Ditlev E

PY - 2023/2

Y1 - 2023/2

N2 - 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.

AB - 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.

KW - Adenosine Triphosphatases/metabolism

KW - Adenosine Triphosphate/metabolism

KW - Escherichia coli/enzymology

KW - Escherichia coli Proteins/metabolism

KW - Organophosphonates/metabolism

U2 - 10.1038/s41467-023-36604-y

DO - 10.1038/s41467-023-36604-y

M3 - Journal article

C2 - 36813778

SN - 2041-1723

VL - 14

JO - Nature Communications

JF - Nature Communications

M1 - 1001

ER -

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

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