High-resolution crystal structure reveals molecular details of target recognition by bacitracin

Proc Natl Acad Sci U S A. 2013 Aug 27;110(35):14207-12. doi: 10.1073/pnas.1308268110. Epub 2013 Aug 12.

Abstract

Bacitracin is a metalloantibiotic agent that is widely used as a medicine and feed additive. It interferes with bacterial cell-wall biosynthesis by binding undecaprenyl-pyrophosphate, a lipid carrier that serves as a critical intermediate in cell wall production. Despite bacitracin's broad use, the molecular details of its target recognition have not been elucidated. Here we report a crystal structure for the ternary complex of bacitracin A, zinc, and a geranyl-pyrophosphate ligand at a resolution of 1.1 Å. The antibiotic forms a compact structure that completely envelopes the ligand's pyrophosphate group, together with flanking zinc and sodium ions. The complex adopts a highly amphipathic conformation that offers clues to antibiotic function in the context of bacterial membranes. Bacitracin's efficient sequestration of its target represents a previously unseen mode for the recognition of lipid pyrophosphates, and suggests new directions for the design of next-generation antimicrobial agents.

Keywords: X-ray crystallography; antibiotic resistance; molecular recognition.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacitracin / chemistry
  • Bacitracin / metabolism*
  • Cell Membrane / metabolism
  • Crystallography, X-Ray
  • Models, Molecular
  • Molecular Sequence Data
  • Polyisoprenyl Phosphates / metabolism
  • Protein Binding
  • Protein Conformation
  • Surface Plasmon Resonance

Substances

  • Polyisoprenyl Phosphates
  • Bacitracin
  • undecaprenyl pyrophosphate
  • bacitracin A

Associated data

  • PDB/4K7T