Journal of Structural Biology, Vol.150, No.1, 50-57, 2005
Trimeric structure of OprN and OprM efflux proteins from Pseudomonas aeruginosa, by 2D electron crystallography
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 1.4nm, respectively. Both proteins present a dense ring of protein density, of similar to 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. (c) 2005 Elsevier Inc. All rights reserved.
Keywords:antibiotic resistance;efflux pumps;outer membrane protein;OprM;OprN;2D electron crystallography;cryo-EM