Fig. 4: Conformational changes in LolCDE upon vanadate trapping.
From: Mechanism of LolCDE as a molecular extruder of bacterial triacylated lipoproteins
a Cryo-EM structure of vanadate-trapped LolCDE with subunits colored as in Fig. 1. b Cross-sectional view perpendicular to the membrane plane indicated in (a). c T-shaped structure formed by the 90° kinks of both TM2 helices. Displacement of the Cα atoms of selected residues is shown. d Propagation of upward movement from coupling helix (CH) to TM2, measured as displacement of Cα atoms of indicated residues. Towards the N-terminal region, both TM2 helices undergo inward movement. The more pronounced inward shift of the TM2 in LolE is highlighted in dotted boxes. e Translation and rotation of the periplasmic domain of LolC is illustrated by comparison of nucleotide-free (gray) and vanadate-trapped (color) LolCDE. Selected structural regions are highlighted and the displacement of Cα atoms of indicated residues shown. f Same as (e), except for the periplasmic domain of LolE. g Top-down view of periplasmic domains showing overall conformational changes. Hook in LolC and the hook counterpart (HC) in LolE are colored magenta.
