3jty

Publication Abstract from PubMed

The X-ray structure of a putative BenF-like (gene name: PFL1329) protein from Pseudomonas fluorescens Pf-5 (PflBenF) has been determined at 2.6A resolution. X-ray crystallography revealed a canonical 18-stranded beta-barrel fold that forms a central pore with a diameter of approximately 4.6A, 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 approximately Asp approximately Arg approximately Arg approximately Ser approximately Asp approximately Arg (R approximately D approximately R approximately R approximately S approximately D approximately R sequence motif, where approximately denotes intervening residues) that define the narrowest part of the pore.

Structure of a putative BenF-like porin from Pseudomonas fluorescens Pf-5 at 2.6 A resolution.,Sampathkumar P, Lu F, Zhao X, Li Z, Gilmore J, Bain K, Rutter ME, Gheyi T, Schwinn KD, Bonanno JB, Pieper U, Fajardo JE, Fiser A, Almo SC, Swaminathan S, Chance MR, Baker D, Atwell S, Thompson DA, Emtage JS, Wasserman SR, Sali A, Sauder JM, Burley SK Proteins. 2010 Nov 1;78(14):3056-62. doi: 10.1002/prot.22829. PMID:20737437^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.