view article

Figure 2
Structural features of TFP pilins. The crystal structure of full-length PilE1 from N. gonorrhoeae (PDB entry 2hi2; Craig et al., 2006BB17) showcasing the distinct domains of TFP pilin proteins: an N-terminal hydrophobic helix (α1) responsible for pilin polymerization, an αβ loop and a D-region. In PilE1 and other TFP pilin structures from Gram-negative bacteria determined to date, the D-region is delimited by a disulfide bond that links the termini of the D-region (Cys121–Cys151 in this case; yellow). This domain exhibits the lowest level of sequence conservation across TFP pilins and contains a hypervariable loop with the highest level of variability.

Journal logoSTRUCTURAL
ISSN: 2059-7983
Follow Acta Cryst. D
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds