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![[Figure 2]](ip5006fig2mag.jpg)
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Figure 2
Structural features of TFP pilins. The crystal structure of full-length PilE1 from N. gonorrhoeae (PDB entry 2hi2; Craig et al., 2006  ) showcasing the distinct domains of TFP pilin proteins: an N-terminal hydrophobic helix (α1) responsible for pilin polymerization, an α–β 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. |
![[Figure 2]](ip5006fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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