Figure 4 | Scientific Reports

Figure 4

From: Conserved amino acid networks modulate discrete functional properties in an enzyme superfamily

Figure 4

Sector definition for the ptRNase superfamily. (a) IC-based sub-matrix of the C i,j coupling matrix displaying the top five ICs, resulting in the definition of two sectors – sector 1 corresponding to IC1 and sector 2, comprised of ICs 2, 3, 4 and 5. Color scheme of the diagonal elements in the matrix correspond to the intrinsic conservation of residues, with red and blue colors corresponding to high and low conservation, respectively. Colors of the off-diagonal elements reflects the correlation between residues with the red end of the spectrum corresponding to strongly correlated residue pairs while the blue end of the spectrum indicates uncorrelated interactions. (b) Two sectors defined based on IC grouping shown in a. (c) Effects of amino acid mutations in sectors 1 (red circles) and 2 (squares) on the catalytic rate (k cat ) relative to wild type and change in thermal stability (ΔT m  = T m(mutant)  − T m(WT) ) in bovine RNase A. The colors of the squares correspond to the IC subgroups defined in Fig. 1. Mutational data were obtained from the literature and are presented for positions where biochemical properties were characterized under the same conditions using polyC as substrate (residues in bold in Table S4). Wild-type data is shown as a black triangle while non-sector residues are displayed as grey triangles.

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