An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane

Trevor F. Moraes, Manjeet Bains, Robert E.W. Hancock, Natalie C.J. Strynadka

Research output: Contribution to journalArticlepeer-review

70 Citations (Scopus)


The outer membrane protein OprP mediates the transport of essential phosphate anions into the pathogenic bacterium Pseudomonas aeruginosa. Here we report the crystallographic structure of trimeric OprP at 1.9-Å resolution, revealing an unprecedented 9-residue arginine 'ladder' that spans from the extracellular surface down through a constriction zone where phosphate is coordinated. Lysine residues coat the inner periplasmic surface, creating an 'electropositive sink' that pulls the phosphates through the eyelet and into the cell.

Original languageEnglish
Pages (from-to)85-87
Number of pages3
JournalNature Structural and Molecular Biology
Issue number1
Publication statusPublished or Issued - Jan 2007
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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