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. Author manuscript; available in PMC: 2020 Jul 18.
Published in final edited form as: J Am Chem Soc. 2018 Dec 27;141(1):290–297. doi: 10.1021/jacs.8b09928

Figure 4. Residues critical for FusA/E/B ternary complex.

Figure 4.

The RRE domain of MccB (residues M1-S86, PDB entry 3H9J, blue) was aligned with FusE. Spheres indicate residues of FusE probed by mutagenesis. Mutagenesis at sites along α3 drastically reduced binding to FusAleader (orange). Ala-substitutions along β2 and β3 did not influence FusAleader binding but did abolish leader peptide cleavage (green). The validity of these predicted protein-protein interaction sites is underscored by the fact mutagenesis elsewhere (gray) did not reduce leader peptide binding or leader peptidase activity.