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Structural insights into the bacterial carbon–phosphorus lyase machinery

Author

Listed:
  • Paulina Seweryn

    (Aarhus University)

  • Lan Bich Van

    (Aarhus University)

  • Morten Kjeldgaard

    (Aarhus University)

  • Christopher J. Russo

    (Medical Research Council Laboratory of Molecular Biology)

  • Lori A. Passmore

    (Medical Research Council Laboratory of Molecular Biology)

  • Bjarne Hove-Jensen

    (Aarhus University)

  • Bjarne Jochimsen

    (Aarhus University)

  • Ditlev E. Brodersen

    (Aarhus University)

Abstract

Phosphorus is required for all life and microorganisms can extract it from their environment through several metabolic pathways. When phosphate is in limited supply, some bacteria are able to use phosphonate compounds, which require specialized enzymatic machinery to break the stable carbon–phosphorus (C–P) bond. Despite its importance, the details of how this machinery catabolizes phosphonates remain unknown. Here we determine the crystal structure of the 240-kilodalton Escherichia coli C–P lyase core complex (PhnG–PhnH–PhnI–PhnJ; PhnGHIJ), and show that it is a two-fold symmetric hetero-octamer comprising an intertwined network of subunits with unexpected self-homologies. It contains two potential active sites that probably couple phosphonate compounds to ATP and subsequently hydrolyse the C–P bond. We map the binding site of PhnK on the complex using electron microscopy, and show that it binds to a conserved insertion domain of PhnJ. Our results provide a structural basis for understanding microbial phosphonate breakdown.

Suggested Citation

  • Paulina Seweryn & Lan Bich Van & Morten Kjeldgaard & Christopher J. Russo & Lori A. Passmore & Bjarne Hove-Jensen & Bjarne Jochimsen & Ditlev E. Brodersen, 2015. "Structural insights into the bacterial carbon–phosphorus lyase machinery," Nature, Nature, vol. 525(7567), pages 68-72, September.
    • Handle: RePEc:nat:nature:v:525:y:2015:i:7567:d:10.1038_nature14683
    DOI: 10.1038/nature14683
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    Cited by:

    1. Qi Zhang & Lu Jia & Yuchen Chen & Hanlu Yan & Qiuwen Chen & Jianmin Zhang & Hao Sun, 2024. "Molecular Mechanisms of the Cyanobacterial Response to Different Phosphorus Sources," Sustainability, MDPI, vol. 16(13), pages 1-14, July.
    2. Dingyi Wang & Mingjie Li & Chengdong Shuang & Yong Liang & Yue Zhao & Minyan Wang & Zhuangzhi Shi, 2022. "Rhodium-catalyzed selective direct arylation of phosphines with aryl bromides," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    3. 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, 2023. "Structural remodelling of the carbon–phosphorus lyase machinery by a dual ABC ATPase," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    4. Michael C. Gilmore & Felipe Cava, 2022. "Peptidoglycan recycling mediated by an ABC transporter in the plant pathogen Agrobacterium tumefaciens," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    5. Leandro Israel da Silva & Marlon Correa Pereira & André Mundstock Xavier de Carvalho & Victor Hugo Buttrós & Moacir Pasqual & Joyce Dória, 2023. "Phosphorus-Solubilizing Microorganisms: A Key to Sustainable Agriculture," Agriculture, MDPI, vol. 13(2), pages 1-30, February.

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