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 1.4 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.
Lambert
Olivier
O
IECB, UMR-CNRS 5471, Université Bordeaux1, 2 rue Robert Escarpit, F-33607 Pessac, France.
Benabdelhak
Houssain
H
Chami
Mohamed
M
Jouan
Ludovic
L
Nouaille
Emilie
E
Ducruix
Arnaud
A
Brisson
Alain
A
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
D001425:Bacterial Outer Membrane Proteins; D026901:Membrane Transport Proteins; C402263:OprM protein, Pseudomonas aeruginosa; C105708:OprN protein, Pseudomonas aeruginosa