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Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae

Author

Listed:
  • Cécile Morlot

    (Université Grenoble Alpes, CNRS, CEA)

  • Daniel Straume

    (Norwegian University of Life Sciences)

  • Katharina Peters

    (Newcastle University)

  • Olav A. Hegnar

    (Norwegian University of Life Sciences)

  • Nolwenn Simon

    (Université Grenoble Alpes, CNRS, CEA)

  • Anne-Marie Villard

    (Université Grenoble Alpes, CNRS, CEA)

  • Carlos Contreras-Martel

    (Université Grenoble Alpes, CNRS, CEA)

  • Francisco Leisico

    (Universidade Nova de Lisboa)

  • Eefjan Breukink

    (Utrecht University)

  • Christine Gravier-Pelletier

    (Université Paris Descartes, Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques UMR 8601 CNRS, Sorbonne Paris Cité (USPC))

  • Laurent Corre

    (Université Paris Descartes, Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques UMR 8601 CNRS, Sorbonne Paris Cité (USPC))

  • Waldemar Vollmer

    (Newcastle University)

  • Nicolas Pietrancosta

    (Université Paris Descartes, Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques UMR 8601 CNRS, Sorbonne Paris Cité (USPC))

  • Leiv Sigve Håvarstein

    (Norwegian University of Life Sciences)

  • André Zapun

    (Université Grenoble Alpes, CNRS, CEA)

Abstract

The universality of peptidoglycan in bacteria underlies the broad spectrum of many successful antibiotics. However, in our times of widespread resistance, the diversity of peptidoglycan modifications offers a variety of new antibacterials targets. In some Gram-positive species such as Streptococcus pneumoniae, Staphylococcus aureus, or Mycobacterium tuberculosis, the second residue of the peptidoglycan precursor, D-glutamate, is amidated into iso-D-glutamine by the essential amidotransferase MurT/GatD complex. Here, we present the structure of this complex at 3.0 Å resolution. MurT has central and C-terminal domains similar to Mur ligases with a cysteine-rich insertion, which probably binds zinc, contributing to the interface with GatD. The mechanism of amidation by MurT is likely similar to the condensation catalyzed by Mur ligases. GatD is a glutaminase providing ammonia that is likely channeled to the MurT active site through a cavity network. The structure and assay presented here constitute a knowledge base for future drug development studies.

Suggested Citation

  • Cécile Morlot & Daniel Straume & Katharina Peters & Olav A. Hegnar & Nolwenn Simon & Anne-Marie Villard & Carlos Contreras-Martel & Francisco Leisico & Eefjan Breukink & Christine Gravier-Pelletier & , 2018. "Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-05602-w
    DOI: 10.1038/s41467-018-05602-w
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