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

Academic Article
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Overview

authors

  • Bayro, M. J.
  • Mukhopadhyay, J.
  • Swapna, G. V. T.
  • Huang, J. Y.
  • Ma, L. C.
  • Sineva, E.
  • Dawson, Philip
  • Montelione, G. T.
  • Ebright, R. H.

publication date

  • 2003

journal

  • Journal of the American Chemical Society  Journal

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.

subject areas

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

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja036677e

PubMed ID

  • 14531661
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Additional Document Info

start page

  • 12382

end page

  • 12383

volume

  • 125

issue

  • 41

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