6FQB

MurT/GatD peptidoglycan amidotransferase complex from Streptococcus pneumoniae R6

Summary for 6FQB

• Entry DOI: 10.2210/pdb6fqb/pdb
• Descriptor: Mur ligase family protein, Cobyric acid synthase, GLUTAMINE (3 entities in total)
• Functional Keywords: mur family, amidotransferase, cytosolic, ligase
• Biological source: Streptococcus pneumoniae; More
• Total number of polymer chains: 8
• Total formula weight: 325234.48

Authors

Morlot, C.,Contreras-Martel, C.,Leisico, F.,Straume, D.,Peters, K.,Hegnar, O.A.,Simon, N.,Villard, A.M.,Breukink, E.,Gravier-Pelletier, C.,Le Corre, L.,Vollmer, W.,Pietrancosta, N.,Havarstein, L.S.,Zapun, A. (deposition date: 2018-02-13, release date: 2018-08-22, Last modification date: 2024-10-23)

Primary citation

Morlot, C.,Straume, D.,Peters, K.,Hegnar, O.A.,Simon, N.,Villard, A.M.,Contreras-Martel, C.,Leisico, F.,Breukink, E.,Gravier-Pelletier, C.,Le Corre, L.,Vollmer, W.,Pietrancosta, N.,Havarstein, L.S.,Zapun, A.
Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae.
Nat Commun, 9:3180-3180, 2018

PubMed 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.

PubMed: 30093673
DOI: 10.1038/s41467-018-05602-w

Experimental method

X-RAY DIFFRACTION (3 Å)