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Crystal structure of MraY, an essential membrane enzyme for bacterial cell wall synthesis.

ABSTRACT: 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.

SUBMITTER: Chung BC 

PROVIDER: S-EPMC3906829 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature

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Crystal structure of MraY, an essential membrane enzyme for bacterial cell wall synthesis.

Chung Ben C BC   Zhao Jinshi J   Gillespie Robert A RA   Kwon Do-Yeon DY   Guan Ziqiang Z   Hong Jiyong J   Zhou Pei P   Lee Seok-Yong SY  

Science (New York, N.Y.) 20130801 6149

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 incl  ...[more]

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