Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2018 Feb 8;8:2600. doi: 10.1038/s41598-018-20925-w

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Comparison of P. aeruginosa PilO structures. (A) Topological diagram of PilO_Δ109 mapping the N- (P110) and C-termini (K206). Helices α1 and α2 are 8 and 13 residues in length, respectively, while β3 and β6 are 12 residues long. Beta strands β1 and β2 are 8 and 3 residues in length, whereas β4 and β5 have 3 and 4 residues, respectively. (B) Comparison of the PilO_Δ109 structure (grey; PDB 5UVR) with the equivalent residues (110–206) of PilO^2RJZ_Δ109 (violet; PDB 2RJZ³⁰). (C) Reverse view of the PilO^2RJZ_Δ109 structure (violet), highlighting the β4 strand residues, D175 and F176 (blue), participating in hydrogen bonding with the β5 strand. (D) The equivalent region of the PilO_Δ109 structure (grey) highlighting the second discontinuous β4β5-strand (inset) and the D175 and F176 residues (blue) not participating in hydrogen bonding with the β6 strand. Hydrogen bonding is indicated by the yellow dashed lines.