Extended Data Fig. 7: Inward-facing conformations of Cgt.
From: Mechanism of cyclic β-glucan export by ABC transporter Cgt of Brucella
a, Alignment of single monomers of CgtAPO (purple) and CgtVAN (yellow), indicating the hinging movement of TM helices 4 and 5 that allows the transition between conformational states. b, Comparison of TM5 of CgtAPO (left) and CgtVAN (right) models. Corresponding density maps are shown. Residues P234 and G244 facilitating the bending of the helix are shown in red. Contour levels are 1.9 and 1.0. c, Alignment of TM5 of Cgt with its structural homologues. Purple, Cgt TM5; blue, TM5 of MsbA (PDB:5tv4); orange, TM11 of ABCB1 (PDB:7a6f). d, Overlay of the CgtSUB cryo-EM density map with the corresponding model at three different angles. An 18-glucose CβG molecule is shown in blue/red. Residues forming the substrate-binding pocket are shown in yellow. Contour levels are 0.25. e, Alignment of Cgt sequences from different species of Rhizobiales focusing on the substrate-binding pocket area. B. abortus residues described in this study are marked with magenta. Sequences corresponding to transmembrane helices are marked in green. Alignment was generated using Geneious. f, Slice-through views of the substrate-bound models of MsbA (PDB:5tv4, left) and CgtSUB (right), indicating distinct substrate-binding mechanisms. Respective substrates are indicated in blue. Unoccupied, inner part of the Cgt central cavity is indicated with blue shading.
