Fig.1
From: A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis
Overall architecture of the FapFβ transporter domain. a Sequence of FapF showing approximate domain boundaries and the construct used for structure solution which consisted of the OmpA signal sequence (SS) and an N-terminal His-Tag (6xH) followed by residues K83–F406 of FapF. b The crystal structure of FapFβ.View from the periplasm through the plane of the membrane and perpendicular to the plane. The lines of three closely packed phenylalanine residues are shown in green space-filling representation, and the small helix plug is shown in blue cartoon representation. Bound detergent molecules in the pore are shown as magenta ball-and-stick representation. The ‘PTG’ motifs (residues P233–G235 and P259–G261) and loop between are shown in red. c Closer view of the constriction site at the top of the helical plug. Conserved residues are shown in stick representation. The pore profile is shown as a surface where blue corresponds to bulk water (radius > 2.3 Å), green is single-file water (1.15–2.3 Å) and red is closed (< 1.15 Å). d The equilibrated position of FapF domain within a coarse-grained asymmetric LPS-containing lipid bilayer
