ATP-binding mode including a carbamoylated lysine and two Mg2+ ions, and substrate-binding mode in Acinetobacter baumannii MurF

Sun Shin Cha, Young Jun An, Chang Sook Jeong, Jeong Hee Yu, Kyung Min Chung

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

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 Mg2+ 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.

Original languageEnglish
Pages (from-to)1045-1050
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume450
Issue number2
DOIs
StatePublished - 25 Jul 2014

Keywords

  • Carbamoylated lysine
  • Crystal structure
  • Magnesium
  • MurF-ATP complex
  • MurF-ATP-UDP complex

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