Coelichelin, a new peptide siderophore encoded by the Streptomyces coelicolor genome: structure prediction from the sequence of its non-ribosomal peptide synthetase

FEMS Microbiol Lett. 2000 Jun 15;187(2):111-4. doi: 10.1111/j.1574-6968.2000.tb09145.x.

Abstract

A gene cluster for the non-ribosomal synthesis of a peptide of unknown structure has been identified in the partial genome sequence of Streptomyces coelicolor. Using molecular and computational analyses, the total structure of a tripeptide siderophore synthesized by the non-ribosomal peptide synthetase within the cluster has been deduced from the translated sequence of its encoding gene. This represents a novel method for the structural assignment of natural products from genome sequence data.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Computational Biology
  • Genome, Bacterial*
  • Molecular Sequence Data
  • Multigene Family
  • Oligopeptides / biosynthesis
  • Oligopeptides / chemistry*
  • Oligopeptides / genetics
  • Peptide Biosynthesis
  • Peptide Synthases / chemistry*
  • Peptide Synthases / genetics*
  • Peptide Synthases / metabolism
  • Protein Structure, Tertiary
  • Siderophores / biosynthesis
  • Siderophores / chemistry*
  • Siderophores / genetics
  • Streptomyces / enzymology
  • Streptomyces / genetics*

Substances

  • Oligopeptides
  • Siderophores
  • coelichelin
  • Peptide Synthases
  • non-ribosomal peptide synthase

Associated data

  • GENBANK/AL109974