4QDI

Crystal structure II of MurF from Acinetobacter baumannii

Summary for 4QDI

• Entry DOI: 10.2210/pdb4qdi/pdb
• Related: 4QF5
• Descriptor: UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase, ADENOSINE-5'-TRIPHOSPHATE, URIDINE-5'-DIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: udp-n-acetylmuramoyl-tripeptide-d-alanyl-d-ananine ligase, ligase
• Biological source: Acinetobacter baumannii
• Cellular location: Cytoplasm : B7GVN5
• Total number of polymer chains: 1
• Total formula weight: 52769.28

Authors

An, Y.J.,Jeong, C.S.,Cha, S.S. (deposition date: 2014-05-13, release date: 2015-04-01, Last modification date: 2024-03-20)

Primary citation

Cha, S.S.,An, Y.J.,Jeong, C.S.,Yu, J.H.,Chung, K.M.
ATP-binding mode including a carbamoylated lysine and two Mg(2+) ions, and substrate-binding mode in Acinetobacter baumannii MurF
Biochem.Biophys.Res.Commun., 450:1045-1050, 2014

PubMed Abstract: MurF adds d-Ala-d-Ala dipeptide to UDP-N-acetylmuramyl-l-Ala-γ-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.

PubMed: 24978312
DOI: 10.1016/j.bbrc.2014.06.108

Experimental method

X-RAY DIFFRACTION (1.8 Å)