Fig. 1 | Nature Communications

Fig. 1

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

Fig. 1The alternative text for this image may have been generated using AI.

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

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