The structure of the cyanobactin domain of unknown function from PatG in the patellamide gene cluster

Greg Mann, Jesko Koehnke, Andrew F. Bent, Rachael Graham, Wael Houssen, Marcel Jaspars, Uli Schwarz-Linek, James H. Naismith*

*Corresponding author for this work

Research output: Contribution to journalArticle

11 Citations (Scopus)
5 Downloads (Pure)

Abstract

Patellamides are members of the cyanobactin family of ribosomally synthesized and post-translationally modified cyclic peptide natural products, many of which, including some patellamides, are biologically active. A detailed mechanistic understanding of the biosynthetic pathway would enable the construction of a biotechnological 'toolkit' to make novel analogues of patellamides that are not found in nature. All but two of the protein domains involved in patellamide biosynthesis have been characterized. The two domains of unknown function (DUFs) are homologous to each other and are found at the C-termini of the multi-domain proteins PatA and PatG. The domain sequence is found in all cyanobactin-biosynthetic pathways characterized to date, implying a functional role in cyanobactin biosynthesis. Here, the crystal structure of the PatG DUF domain is reported and its binding interactions with plausible substrates are investigated.

Original languageEnglish
Pages (from-to)1597-1603
Number of pages7
JournalActa Crystallographica Section F: Structural Biology Communications
Volume70
Issue number12
Early online dateNov 2014
DOIs
Publication statusPublished - Dec 2014

Keywords

  • LISSOCLINUM-PATELLA
  • PROCHLORON-DIDEMNI
  • PROTEIN-STRUCTURE
  • ALIGNMENT
  • PATHWAY
  • SINGLE
  • SYSTEM

Cite this