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

Ben C Chung1, Jinshi Zhao1, Robert A Gillespie1

  • 1Department of Biochemistry, Duke University Medical Center, 2 Genome Ct, Durham, NC 27710, USA.

Science (New York, N.Y.)
|August 31, 2013
PubMed

Insights

Researchers determined the crystal structure of MraY (phospho-MurNAc-pentapeptide translocase), an essential bacterial enzyme. This breakthrough provides a structural basis for understanding MraY and related enzymes, aiding antibiotic development.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • MraY (phospho-MurNAc-pentapeptide translocase) is a key integral membrane enzyme in bacterial cell wall biosynthesis.
  • It catalyzes the transfer of peptidoglycan precursors to lipid carriers, a crucial step for bacterial survival.
  • MraY is a potential target for novel antibiotic development due to its essential role.

Purpose of the Study:

  • To elucidate the structure of MraY to understand its catalytic mechanism.
  • To provide insights into the broader enzyme superfamily involved in glycosylation and cell wall synthesis.
  • To facilitate structure-based drug design for new antibiotics targeting MraY.

Main Methods:

  • X-ray crystallography was employed to determine the structure of MraY from Aquifex aeolicus (MraYAA).
  • The structure was resolved at 3.3 Å resolution.
  • Analysis focused on the enzyme's overall architecture and active site features, including magnesium ion localization.

Main Results:

  • The crystal structure of MraYAA was successfully determined.
  • The overall architecture of the enzyme was visualized.
  • The location of a magnesium ion (Mg2+) within the active site was identified, offering clues to the catalytic mechanism.

Conclusions:

  • The determined MraY structure provides the first structural basis for understanding the catalysis of this essential enzyme.
  • This structural information is vital for mechanistic studies of MraY and its superfamily.
  • The findings pave the way for rational design of inhibitors targeting MraY as potential antibiotics.

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