Structure of a Putative BenF-like Porin From Pseudomonas Fluorescens Pf-5 at 2.6 A Resolution

Proteins. 2010 Nov 1;78(14):3056-62. doi: 10.1002/prot.22829.

Abstract

The X-ray structure of a putative BenF-like (gene name: PFL1329) protein from Pseudomonas fluorescens Pf-5 (PflBenF) has been determined at 2.6Å resolution. X-ray crystallography revealed a canonical 18-stranded β-barrel fold that forms a central pore with a diameter of ∼4.6Å, which is consistent with the size and physicochemical properties of the presumed aromatic acid substrate, benzoate. Detailed comparisons with the previously-determined structure of Pseudomonas aeruginosa OpdK, a vanillate influx channel, revealed an arginine-rich aromatic acid selectivity filter of nearly identical structure composed of seven highly conserved residues Arg∼Asp∼Arg∼Arg∼Ser∼Asp∼Arg (R∼D∼R∼R∼S∼D∼R sequence motif, where ∼ denotes intervening residues) that define the narrowest part of the pore.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Benzoates / metabolism*
  • Crystallography, X-Ray
  • Ion Channels / chemistry*
  • Ion Channels / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Porins / chemistry*
  • Porins / metabolism
  • Protein Conformation
  • Pseudomonas fluorescens / metabolism*
  • Sequence Homology, Amino Acid

Substances

  • Benzoates
  • Ion Channels
  • Porins