Structure of a putative BenF‐like porin from Pseudomonas fluorescens Pf‐5 at 2.6 Å resolution
Year: 2010
Type: article
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.
DOI: 10.1002/prot.22829
Authors: Parthasarathy Sampathkumar, Frances Lu, Xun Zhao, Zhenzhen Li, Jeremiah Gilmore, Kevin Bain, Marc E. Rutter, Tarun Gheyi, Kenneth D. Schwinn, Jeffrey B. Bonanno, Ursula Pieper, J. Eduardo Fajardo, Andras Fiser, Steven C. Almo, Subramanyam Swaminathan, Mark R. Chance, David Baker, Shane Atwell, Devon A. Thompson, J. Spencer Emtage, Stephen R. Wasserman, Andrej Sali, J. Michael Sauder, Stephen K. Burley
Language: English
Subfield: Materials Chemistry
Field: Materials Science
Domain: Physical Sciences
Open Access status: bronze
OpenAlex ID: W2040293462