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Structures of the multi-domain oxygen sensor DosP: remote control of a c-di-GMP phosphodiesterase by a regulatory PAS domain

Author

Listed:
  • Wenbi Wu

    (University of Texas Southwestern Medical Center)

  • Pankaj Kumar

    (University of Texas Southwestern Medical Center)

  • Chad A. Brautigam

    (University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center)

  • Shih-Chia Tso

    (University of Texas Southwestern Medical Center)

  • Hamid R. Baniasadi

    (University of Texas Southwestern Medical Center)

  • Daniel L. Kober

    (University of Texas Southwestern Medical Center)

  • Marie-Alda Gilles-Gonzalez

    (University of Texas Southwestern Medical Center)

Abstract

The heme-based direct oxygen sensor DosP degrades c-di-GMP, a second messenger nearly unique to bacteria. In stationary phase Escherichia coli, DosP is the most abundant c-di-GMP phosphodiesterase. Ligation of O2 to a heme-binding PAS domain (hPAS) of the protein enhances the phosphodiesterase through an allosteric mechanism that has remained elusive. We determine six structures of full-length DosP in its aerobic or anaerobic conformations, with or without c-di-GMP. DosP is an elongated dimer with the regulatory heme containing domain and phosphodiesterase separated by nearly 180 Å. In the absence of substrate, regardless of the heme status, DosP presents an equilibrium of two distinct conformations. Binding of substrate induces DosP to adopt a single, ON-state or OFF-state conformation depending on its heme status. Structural and biochemical studies of this multi-domain sensor and its mutants provide insights into signal regulation of second-messenger levels.

Suggested Citation

  • Wenbi Wu & Pankaj Kumar & Chad A. Brautigam & Shih-Chia Tso & Hamid R. Baniasadi & Daniel L. Kober & Marie-Alda Gilles-Gonzalez, 2024. "Structures of the multi-domain oxygen sensor DosP: remote control of a c-di-GMP phosphodiesterase by a regulatory PAS domain," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-53942-7
    DOI: 10.1038/s41467-024-53942-7
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    1. Xueliang Zhan & Kuo Zhang & Chenchen Wang & Qiao Fan & Xiujia Tang & Xi Zhang & Ke Wang & Yang Fu & Haihua Liang, 2024. "Author Correction: A c-di-GMP signaling module controls responses to iron in Pseudomonas aeruginosa," Nature Communications, Nature, vol. 15(1), pages 1-1, December.
    2. Xueliang Zhan & Kuo Zhang & Chenchen Wang & Qiao Fan & Xiujia Tang & Xi Zhang & Ke Wang & Yang Fu & Haihua Liang, 2024. "A c-di-GMP signaling module controls responses to iron in Pseudomonas aeruginosa," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
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