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Biochem Biophys Res Commun. 2014 Jul 25;450(2):1045-50. doi: 10.1016/j.bbrc.2014.06.108. Epub 2014 Jun 27.

ATP-binding mode including a carbamoylated lysine and two Mg(2+) ions, and substrate-binding mode in Acinetobacter baumannii MurF.

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  • 1Marine Biotechnology Research Division, Korea Institute of Ocean Science and Technology, Ansan 426-744, Republic of Korea; Department of Convergence Study on the Ocean Science and Technology, Ocean Science and Technology School, Pusan 606-791, Republic of Korea; Department of Marine Biotechnology, Korea University of Science and Technology, Daejeon 305-333, Republic of Korea. Electronic address: chajung@kiost.ac.
  • 2Marine Biotechnology Research Division, Korea Institute of Ocean Science and Technology, Ansan 426-744, Republic of Korea.
  • 3Department of Microbiology and Immunology, Chonbuk National University Medical School, Jeonju 561-756, Republic of Korea.
  • 4Department of Microbiology and Immunology, Chonbuk National University Medical School, Jeonju 561-756, Republic of Korea; Institute for Medical Science, Chonbuk National University Medical School, Jeonju 561-756, Republic of Korea. Electronic address: kmin@jbnu.ac.kr.

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.

Copyright © 2014 Elsevier Inc. All rights reserved.

KEYWORDS:

Carbamoylated lysine; Crystal structure; Magnesium; MurF–ATP complex; MurF–ATP–UDP complex

PMID:
24978312
[PubMed - indexed for MEDLINE]
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