Fig. 1
From: Multiple conformations facilitate PilT function in the type IV pilus

PilT from G. metallireducens (PilTGm) crystallizes in multiple conformations. Individual packing units (N2Dn and CTDn+1) are uniquely colored. A smoothed transparent surface representation of the main chain is shown. The ligand bound in the nucleotide-binding site is shown in stick representation. a, c, e, g, j Top and side views of unique PilTGm crystal structures. O and C denote open and closed interfaces, respectively. b, d, f, h, k Correspond to the hexamers shown above and show a cross section of the closed- and open interfaces on the top and bottom panels, respectively. Select side chains discussed in the text are shown for reference. 2|FO|−|Fc| maps are shown as a mesh with I/σ(I) levels of 2 with the exception of (d) where 1.5 was used. a, b Crystal structure of methylated PilTGm in the OCOCOC conformation. c, d Crystal structure of PilTGm without added nucleotide in the OCOCOC conformation. e, f Crystal structure of PilTGm washed with ATP prior to crystallization in the OCOCOC conformation. g, h Crystal structure of PilTGm incubated with ATP during crystallization at pH 6.5 in the CCCCCC conformation. i In vitro ATP hydrolysis (mean ± SEM, n = 2) by PilTGm from pH 5.5 to 9.0. j, k Crystal structure of PilTGm incubated with ANP during crystallization in the CCOCCO conformation