title: Structural insight into OprD substrate specificity.
abstract: OprD proteins form a large family of substrate-specific outer-membrane channels in Gram-negative bacteria. We report here the X-ray crystal structure of OprD from Pseudomonas aeruginosa, which reveals a monomeric 18-stranded beta-barrel characterized by a very narrow pore constriction, with a positively charged basic ladder on one side and an electronegative pocket on the other side. The location of highly conserved residues in OprD suggests that the structure represents the general architecture of OprD channels.
authors.affiliation: Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA.
authors.forename: Shyamasri
authors.initials: S
authors.lastname: Biswas
authors.forename: Mohammad M
authors.initials: MM
authors.lastname: Mohammad
authors.forename: Dimki R
authors.initials: DR
authors.lastname: Patel
authors.forename: Liviu
authors.initials: L
authors.lastname: Movileanu
authors.forename: Bert
authors.initials: B
authors.lastname: van den Berg
mesh_terms: D018360:Crystallography, X-Ray; D004594:Electrophysiology; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D018272:Porins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011550:Pseudomonas aeruginosa / Q000737:chemistry*; D013379:Substrate Specificity
chemical_list: D018272:Porins; C077157:OprD protein, Pseudomonas aeruginosa