Structure of Mycobacterium tuberculosis nucleoside diphosphate kinase R80N mutant in complex with citrate

PDB reference: nucleoside diphosphate kinase, R80N mutant, 4ane

Figure S1. Thermal denaturation. The R80N mutant decreased by 8 degrees Celcius and behaves more similarly to the wild-type protein than to the D93N mutation, for which a dramatic decrease of 28 degrees Celcius was observed. The temperature dependence of the excess molar heat capacity of wild-type Mt-NDPK (full circles), the R80N mutant (open squares) and the D93N mutant (full squares) is shown. Each differential scanning calorimetry curve displays a single calorimetric peak. The protein concentration was 0.2-0.3 mg ml-1. DOI: 10.1107/S2053230X13034134/hv5248sup1.jpg

Figure S2. Denaturation/renaturation by urea/GuHCl of wild-type and R80N mutant Mt-NDPK. The unfolding and the loss of quaternary structure are indicated by the excess heat and the enzymatic activity, respectively. Unfolding (full squares) and subsequent refolding (open squares) were monitored by following the intrinsic fluorescence of Mt-NDPK (A in urea, B in GuHCl) and R80N mutant (C in urea, D in GuHCl). The residual enzymatic activity for the unfolding is shown by open circles. The protein concentration was 10 mg ml-1. The measurements are normalized to the maxima; fn is the fraction of native protein. DOI: 10.1107/S2053230X13034134/hv5248sup2.jpg

Figure S3. Binding scheme of citrate in chain A of D80N mutant Mt-NDPK. The figure was drawn with LigPlot+ (Laskowski and Swindells, 2011). DOI: 10.1107/S2053230X13034134/hv5248sup3.pdf

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