Crystal structure of MraY, an essential membrane enzyme for bacterial cell wall synthesis.
Publication Type:Journal Article
Source:Science, Volume 341, Issue 6149, p.1012-1016 (2013)
Keywords:Bacteria, Bacterial Proteins, Catalytic Domain, Cell Wall, Crystallography, X-Ray, Cytoplasm, Membrane Proteins, Periplasm, Protein Conformation, Protein Structure, Secondary, Transferases
<p>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 Mg(2+) within the active site, and provide a structural basis of catalysis for this class of enzyme. </p>