title: Trimeric structure of OprN and OprM efflux proteins from Pseudomonas aeruginosa, by 2D electron crystallography.
abstract: OprM and OprN belong to the outer membrane factor family of multidrug efflux proteins from Pseudomonas aeruginosa, a bacterium responsible of nosocomial infections. We report here the two-dimensional (2D) crystallization of OprN and OprM into lipid bilayers and the determination of their 2D projected structure by cryo-electron crystallography, at 1 and 1.4 nm, respectively. Both proteins present a dense ring of protein density, of approximately 7 nm diameter. An additional thin peripheral ring is resolved in OprN structure. Both proteins are assembled as trimers. The results presented here indicate a high structural homology between OprN (and OprM) and TolC, a multidrug efflux protein from Escherichia coli.
authors.affiliation: IECB, UMR-CNRS 5471, Université Bordeaux1, 2 rue Robert Escarpit, F-33607 Pessac, France.
authors.forename: Olivier
authors.initials: O
authors.lastname: Lambert
authors.forename: Houssain
authors.initials: H
authors.lastname: Benabdelhak
authors.forename: Mohamed
authors.initials: M
authors.lastname: Chami
authors.forename: Ludovic
authors.initials: L
authors.lastname: Jouan
authors.forename: Emilie
authors.initials: E
authors.lastname: Nouaille
authors.forename: Arnaud
authors.initials: A
authors.lastname: Ducruix
authors.forename: Alain
authors.initials: A
authors.lastname: Brisson
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003461:Crystallography; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D008854:Microscopy, Electron; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000378:metabolism
chemical_list: D001425:Bacterial Outer Membrane Proteins; D026901:Membrane Transport Proteins; C402263:OprM protein, Pseudomonas aeruginosa; C105708:OprN protein, Pseudomonas aeruginosa