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. Author manuscript; available in PMC: 2011 Aug 21.
Published in final edited form as: Nature. 2010 Aug 1;466(7309):996–1000. doi: 10.1038/nature09300

Figure 1. Structural overview of the full-length FliG monomer.

Figure 1

a–c, Residues are coloured from N to C terminus as a spectrum of colours from blue to red. Torque helixC5 and helixN3 are labelled with a red and blue asterisk respectively. HelicesC3–6 are shown with charged residues and the electrostatic potential on helixC5 in b adjacent to helicesN1–4 in c to highlight the conserved fold. d, Sequence alignment of the residues shown in b and c. Conserved or similar residues are highlighted, and conserved amino acid triads are underlined. HelixC5 and helixN3 are encircled and charged residues on these helices are in red (negative) and blue (positive).