Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export

By V. Koronakis, A. Sharff, E. Koronakis, B. Luisi, C. Hughes. Nature, 2000

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Computational design of water-soluble α-helical barrels (2014, background): “The few current examples include: natural parallel 5- and 10-helix structures, and antiparallel 10- and 12-helix bundles (17-20); a de novo parallel hexamer, achieved partly serendipitously (21); and a mutant leucine-zipper peptide that forms an unusual staggered parallel 7-helix arrangement (22).”
The TetR Family of Transcriptional Repressors (2005, background): “extrusion of substrates into the medium (102, 193).”
Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems (2008, background): “In gram-negative organisms, three protomers of the OMF protein join to form a single -barrel that spans the outer membrane and a channel of 30 Å in diameter that is bounded by long helical coiled coils and extends into the periplasm (1, 254) (Fig.”
The versatile β-barrel membrane protein (2003, background): “TolC is unique among known b-barrel structures, comprising a trimeric, 12-stranded single barrel [55] in which each monomer contributes four strands to the barrel.”