Structure of bacteriocin AS-48: from soluble state to membrane bound state

J Mol Biol. 2003 Nov 28;334(3):541-9. doi: 10.1016/j.jmb.2003.09.060.


The bacteriocin AS-48 is a membrane-interacting peptide, which displays a broad anti-microbial spectrum against Gram-positive and Gram-negative bacteria. The NMR structure of AS-48 at pH 3 has been solved. The analysis of this structure suggests that the mechanism of AS-48 anti-bacterial activity involves the accumulation of positively charged molecules at the membrane surface leading to a disruption of the membrane potential. Here, we report the high-resolution crystal structure of AS-48 and sedimentation equilibrium experiments showing that this bacteriocin is able to adopt different oligomeric structures according to the physicochemical environment. The analysis of these structures suggests a mechanism for molecular function of AS-48 involving a transition from a water-soluble form to a membrane-bound state upon membrane binding.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins*
  • Cell Membrane / metabolism
  • Crystallography, X-Ray
  • Gram-Positive Bacteria / chemistry*
  • Gram-Positive Bacteria / genetics
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Structure
  • Peptides / chemistry*
  • Peptides / metabolism
  • Protein Conformation*
  • Water / chemistry


  • Bacterial Proteins
  • Peptides
  • Water
  • BacA protein, Enterococcus faecalis

Associated data

  • PDB/1O82
  • PDB/1O83
  • PDB/1O84