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. 2016 Mar 29;291(21):10950–10960. doi: 10.1074/jbc.M116.715912

FIGURE 5.

FIGURE 5.

Inhibition of EcMazF by EcMazE(68–82). A, hydrogen bonding around Glu-24. In the EcMazF-d(AUACAUA) complex, the side chain of Glu-24 does not interact with the ligand. Rather, this side chain is buried, and its negative charge is neutralized by salt bridges with the side chains of Arg-86 and Lys-79. The EcMazF is represented as a schematic with one subunit colored green and the other cyan. B, electron density for the EcMazE(68–82) peptide. The different amino acid residues are labeled. C, superposition of the EcMazF dimers as seen in the d(AUACAUA) complex (green and cyan as in A) and the EcMazE(68–82) complex (yellow). The EcMazE(68–82) is shown in red. Relevant amino acid side chains are shown as sticks and are labeled. Glu-80 of EcMazE(68–82) in the peptide complex takes over the role of Glu-24 of EcMazF in the d(AUACAUA) complex.