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. 2021 Apr 28;121(9):5479–5596. doi: 10.1021/acs.chemrev.1c00055

Figure 29.

Figure 29

(A) Highlight of the conserved amino acids among 5 OMFs. The protomeric structures of TolC (1EK9, blue), OprM (3D5K, purple), VceC (1YC9, ochre), CmeC (4MT4, green), and CusC (3PIK, red) are shown in the upper part of the panel. The side chains of the preserved residues are represented as spheres of different colors according to their intrinsic location in the protein: orange for the β-barrel part, green for the equatorial part, and blue for the periplasmic part. The position of each conserved amino acid within the primary sequence is shown in the table in the lower part of the panel. (B) Visualization of the β-barrel domains within the quaternary structures of 5 OMFs. Each porin retains the same structural color as in panel A. Two views are shown: a side view first and a top view second.