Crystal structure of halogenase PltA from the pyoluteorin biosynthetic pathway

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27 Scopus citations

Abstract

Pyoluteorin is an antifungal agent composed of a 4,5-dichlorinated pyrrole group linked to a resorcinol moiety. The pyoluteorin biosynthetic gene cluster in Pseudomonas fluorescens Pf-5 encodes the halogenase PltA, which has been previously demonstrated to perform both chlorinations in vitro. PltA selectively accepts as a substrate a pyrrole moiety covalently tethered to a nonribosomal peptide thiolation domain PltL (pyrrolyl- S-PltL) for FAD-dependent di-chlorination, yielding 4,5-dichloropyrrolyl- S-PltL. We report a 2.75 Å-resolution crystal structure of PltA in complex with FAD and chloride. PltA is a dimeric enzyme, containing a flavin-binding fold conserved in flavin-dependent halogenases and monooxygenases, and an additional unique helical region at the C-terminus. This C-terminal region blocks a putative substrate-binding cleft, suggesting that a conformational change involving repositioning of this region is necessary to allow binding of the pyrrolyl- S-PltL substrate for its dichlorination by PltA.

Original languageEnglish
Pages (from-to)349-357
Number of pages9
JournalJournal of Structural Biology
Volume192
Issue number3
DOIs
StatePublished - Dec 2015

Bibliographical note

Publisher Copyright:
© 2015 Elsevier Inc.

Keywords

  • Chlorination
  • FAD
  • Flavoprotein
  • Halogenation
  • Natural product

ASJC Scopus subject areas

  • Structural Biology

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