Crystal Structure of MraY, an Essential Membrane Enzyme for Bacterial Cell Wall Synthesis

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Science  30 Aug 2013:
Vol. 341, Issue 6149, pp. 1012-1016
DOI: 10.1126/science.1236501

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Moving Bricks with MraY

Peptidoglycan, the building brick of bacterial cell walls, is synthesized in the cytoplasm and must be transported across the cell membrane. To achieve this, it is attached to a carrier lipid by the integral membrane protein MraY. MraY is targeted by natural antibacterials and is a promising antibiotic target. Chung et al. (p. 1012) report the crystal structure of MraY at 3.3 Å resolution. The structure, together with mutational mapping, outlines the location of the active site and provides interesting hints for how the enzyme binds the substrate and catalyzes attachment to the carrier lipid.


MraY (phospho-MurNAc-pentapeptide translocase) is an integral membrane enzyme that catalyzes an essential step of bacterial cell wall biosynthesis: the transfer of the peptidoglycan precursor phospho-MurNAc-pentapeptide to the lipid carrier undecaprenyl phosphate. MraY has long been considered a promising target for the development of antibiotics, but the lack of a structure has hindered mechanistic understanding of this critical enzyme and the enzyme superfamily in general. The superfamily includes enzymes involved in bacterial lipopolysaccharide/teichoic acid formation and eukaryotic N-linked glycosylation, modifications that are central in many biological processes. We present the crystal structure of MraY from Aquifex aeolicus (MraYAA) at 3.3 Å resolution, which allows us to visualize the overall architecture, locate Mg2+ within the active site, and provide a structural basis of catalysis for this class of enzyme.

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