Structural aspects of non-ribosomal peptide biosynthesis

G L Challis, James Henderson Naismith

Research output: Contribution to journalArticlepeer-review

92 Citations (Scopus)

Abstract

Small peptides have powerful biological activities ranging from antibiotic to immune suppression. These peptides are synthesized by non-ribosomal peptide synthetases (NRPS). Structural understanding of NRPS took a huge leap forward in 2002; this information has led to several detailed biochemical studies and further structural studies. NRPS are complex molecular machines composed of multiple modules and each module contains several autonomously folded catalytic domains. Structural studies have largely focused on individual domains, isolated from the context of the multienzyme. Biochemical studies have looked at individual domains, isolated whole modules and intact NRPS, and the combined data begin to allow us to visualize the process of peptide assembly by NRPS.

Original languageEnglish
Pages (from-to)748-756
Number of pages9
JournalCurrent Opinion in Structural Biology
Volume14
DOIs
Publication statusPublished - Dec 2004

Keywords

  • INITIATION MODULE PHEATE
  • TYROCIDINE SYNTHETASE
  • THIOESTERASE DOMAIN
  • CRYSTAL-STRUCTURE
  • GRAMICIDIN-S
  • YERSINIABACTIN SYNTHETASE
  • VIBRIOBACTIN SYNTHETASE
  • SUBSTRATE RECOGNITION
  • CONDENSATION DOMAINS
  • ADENYLATION DOMAINS

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