Fig. 6: Oep80β C587S/S408C crosslinks efficiently with Oep21a β-1 KtoC but not Oep21a β-1 CterC, indicating anti-parallel binding to Oep80’s β1 strand. | Communications Biology

Fig. 6: Oep80β C587S/S408C crosslinks efficiently with Oep21a β-1 KtoC but not Oep21a β-1 CterC, indicating anti-parallel binding to Oep80’s β1 strand.

From: Biochemical characterisation supports a central role for Oep80 from Arabidopsis thaliana in chloroplastic β-barrel protein assembly

Fig. 6

a Schematic showing the experimental strategy. Oep80β C587S/S408C combined with mutant Oep21a β-1 peptides containing cysteines on either end enables differentiation between parallel and antiparallel signal peptide binding. Green arrow represents peptide; red circles represent introduced cysteine residues and the yellow lines represent disulfide bonds. b AlphaFold 3 model of Oep80β C587S/S408C plus Oep21a β-1 KtoC. The inset shows the interaction interface in detail. Peptide backbone in green, Oep80 barrel backbone in cyan. Mutant residues coloured red. Dotted lines in the inset indicate likely hydrogen bonding interactions. c Oep80β S048C/C587S alone or plus either peptide was incubated at 4 °C with 0.1 mM CuSO4. Samples were taken after 3 h (3 h) or overnight (O/N). DTT (+) indicates the sample was boiled with 50 mM DTT in loading dye.

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