Structure of antibacterial peptide microcin J25: a 21-residue lariat protoknot

J Am Chem Soc. 2003 Oct 15;125(41):12382-3. doi: 10.1021/ja036677e.

Abstract

The antibacterial peptide microcin J25 (MccJ25) inhibits bacterial transcription by binding within, and obstructing, the nucleotide-uptake channel of bacterial RNA polymerase. Published covalent and three-dimensional structures indicate that MccJ25 is a 21-residue cycle. Here, we show that the published covalent and three-dimensional structures are incorrect, and that MccJ25 in fact is a 21-residue "lariat protoknot", consisting of an 8-residue cyclic segment followed by a 13-residue linear segment that loops back and threads through the cyclic segment. MccJ25 is the first example of a lariat protoknot involving a backbone-side chain amide linkage.

Publication types

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

MeSH terms

  • Anti-Bacterial Agents / chemistry
  • Bacteriocins / chemistry*
  • Models, Molecular
  • Peptides
  • Protein Conformation
  • Spectrometry, Mass, Electrospray Ionization

Substances

  • Anti-Bacterial Agents
  • Bacteriocins
  • Peptides
  • microcin