Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae - Archive ouverte HAL
Article Dans Une Revue Nature Communications Année : 2018

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

Cécile Morlot
Daniel Straume
  • Fonction : Auteur
Katharina Peters
  • Fonction : Auteur
Olav A Hegnar
  • Fonction : Auteur
Nolwenn Simon
  • Fonction : Auteur
Francisco Leisico
  • Fonction : Auteur
Waldemar Vollmer
Leiv Sigve Håvarstein
  • Fonction : Auteur
André Zapun

Résumé

The universality of peptidoglycan in bacteria underlies the broad spectrum of many successful antibiotics. However, in our times of widespread resistance, the diversity of pepti-doglycan 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.
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Dates et versions

hal-01861372 , version 1 (24-08-2018)

Identifiants

Citer

Cécile Morlot, Daniel Straume, Katharina Peters, Olav A Hegnar, Nolwenn Simon, et al.. Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae. Nature Communications, 2018, 9, pp.3180. ⟨10.1038/s41467-018-05602-w⟩. ⟨hal-01861372⟩
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