D-Glutamic acid is a required biosynthetic building block for peptidoglycan, and the enzyme glutamate racemase (GluR) catalyzes the inter-conversion of D and L-glutamate enantiomers. Therefore, GluR is considered as an attractive target for the design of new antibacterial drugs. Here, we report the crystal structure of GluR from Francisella tularensis subsp. tularensis SCHU S4 in complex with D-glutamate, which provides a basis for designing narrow-spectrum antimicrobial agents.
Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan