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

Cécile Morlot, Daniel Straume, Katharina Peters, Olav A. Hegnar, Nolwenn Simon, Anne-Marie Villard, Carlos Contreras-Martel, Francisco Leisico, Eefjan Breukink, Christine Gravier-Pelletier, Laurent Corre, Waldemar Vollmer, Nicolas Pietrancosta, Leiv Sigve Håvarstein and André Zapun ()
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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

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-05602-w

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