Article Figures & Data
Figures
- Fig. 1.
Histograms of single-channel conductance measurements showing channel size distributions for OprF (A) and OprF1–162 (B).
- Fig. 2.
CD spectral analysis of OprF1–162 in 0.1% sodium dodecyl sulfate.
- Fig. 3.
Alignment of the sequences of OprF1–162 and OmpA1–171, according to sequence hydrophobicity and location of charged residues (see the text). Predicted transmembrane regions are boxed, and stars mark identical residues. The two underlined tryptophans are examples of residues conserved in location in three-dimensional space (according to our modeling) but not conserved in location along the sequence.
- Fig. 4.
Three-dimensional model of OprF1–162, constructed by threading the sequence of OprF1–162 on a crystal structure of OmpA1–171. (A) Overview of the molecule, highlighting all aromatic residues on the outside of the protein (yellow). Note the striking rings of aromatic residues at the proposed water-lipid interfaces. (B) A slice horizontally through the barrel of the proposed model of OprF (blue), overlaid on the structure of OmpA (yellow), illustrating how residues previously proposed to form a barrier to pore formation in OmpA (12) are not conserved in OprF and allow for a larger channel with no salt bridge in that region.
