We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae.
- Authors
Morlot, Cécile; Straume, Daniel; Peters, Katharina; Hegnar, Olav A.; Simon, Nolwenn; Villard, Anne-Marie; Contreras-Martel, Carlos; Leisico, Francisco; Breukink, Eefjan; Gravier-Pelletier, Christine; Le Corre, Laurent; Vollmer, Waldemar; Pietrancosta, Nicolas; Håvarstein, Leiv Sigve; Zapun, André
- 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.
- Publication
Nature Communications, 2018, Vol 9, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-018-05602-w