Fig. 4: Five positively charged residues provide critical binding interactions and another six make important contributions. | Nature Communications

Fig. 4: Five positively charged residues provide critical binding interactions and another six make important contributions.

From: Substrate binding in the mitochondrial ADP/ATP carrier is a step-wise process guiding the structural changes in the transport cycle

Fig. 4

a, b Thermostability shift values (ΔTm) determined at 0.1, 0.5, 1, 5, 10 mM substrate concentration for the wild type and single alanine replacement variants. Circles and error bars represent the mean and standard deviation of eight independent experiments for the wild type and 3–7 for the variants. Empty and filled circles represent ADP and ATP, respectively. Data for the wild-type protein are shown in black, whereas those for the variants are shown in red (a) or in orange (b) for the critical and important residues, respectively. Note that for several data points the mean value and error bars of ADP vs ATP groups are identical and consequently their graphical representation is superimposed, with the ADP marker on top. Error bars are sometimes masked by the symbol. Significant differences were evaluated by two-way ANOVA with interaction, as described in “Methods”. Significant values (p ≤ 0.01) are indicated by * or # for ADP and ATP, respectively. c TtAac matrix-open BKA-bound structure (PDB code: 6gci chain A) (left) and close-up view (right) showing the analysed residues in red or orange stick and sphere for Gly representations. Helices are shown in wheat cartoon representation and are labelled. Source data for this figure are provided as a Source Data file.

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