4qdi

Publication Abstract from PubMed

MurF adds d-Ala-d-Ala dipeptide to UDP-N-acetylmuramyl-l-Ala-gamma-d-Glu-m-DAP (or l-Lys) in an ATP-dependent manner, which is the last step in the biosynthesis of monomeric precursor of peptidoglycan. Here we report crystal structures of two MurF-ATP complexes: the MurF-ATP complex and the MurF-ATP-UDP complex. The ATP-binding mode revealed by the crystal structure of the MurF-ATP complex confirms the previous biochemical demonstration that a carbamoylated lysine and two Mg(2+) ions are required for enzyme activity of MurF. The UDP-MurF interactions observed in the crystal structure of the MurF-ATP-UDP complex depict the characteristic substrate-binding mode of MurF. The emergence and dissemination of multidrug-resistant Acinetobacter baumannii strains are great threats to public health. Therefore, the structural information on A. baumannii MurF as a validated target for drug discovery will provide a framework to develop antibacterial agents against multidrug-resistant A. baumannii infections as well as to understand the reaction mechanism of MurF.

ATP-binding mode including a carbamoylated lysine and two Mg(2+) ions, and substrate-binding mode in Acinetobacter baumannii MurF.,Cha SS, An YJ, Jeong CS, Yu JH, Chung KM Biochem Biophys Res Commun. 2014 Jul 25;450(2):1045-50. doi:, 10.1016/j.bbrc.2014.06.108. Epub 2014 Jun 27. PMID:24978312^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.