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- W2885468091 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." @default.
- W2885468091 created "2018-08-22" @default.
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- W2885468091 date "2018-08-09" @default.
- W2885468091 modified "2023-10-15" @default.
- W2885468091 title "Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae" @default.
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- W2885468091 doi "https://doi.org/10.1038/s41467-018-05602-w" @default.
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- W2885468091 hasPublicationYear "2018" @default.
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