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. 2020 May 27;9:e53853. doi: 10.7554/eLife.53853

Figure 5. Mutagenesis screen for residues essential for the function of the β subunit.

(a) Structure of the β subunit cytoplasmic face. Highly conserved residues with polar or charged side chains are highlighted. Residues with red and underlined labels were characterized by our study and previous studies on KpOAD, respectively. The ′ and ″ signs indicate residues in the second (yellow) and third (gray) β subunits in the complex, respectively. The black cycle indicates the putative sodium binding cavity. (b) Oxaloacetate decarboxylation by StOAD with substitutions in the β subunit cytoplasmic face. Data for the wild type complex is shown for comparison. (c) ITC experiments probing sodium binding to StOAD βγ sub-complex with substitutions in the β subunit cytoplasmic face. Data for the wild type complex is shown for comparison.

Figure 5—source data 1. Summary of OAD activity experiments.
Figure 5—source data 2. Summary of ITC experiments.

Figure 5.

Figure 5—figure supplement 1. Thermograms of ITC experiments probing sodium binding to the StOAD βγ sub-complex.

Figure 5—figure supplement 1.

Substitutions were introduced on residues selected for the mutagenesis screen.