Pheromone Recognition and Selectivity by ComR Proteins among Streptococcus Species
Fig 5
The molecular surface properties of apo-ComR S. suis.
(A) Solvent accessible surface representation colored by amino-acid conservation using the Consurf server and the bacterial strains used in this study. Darker red indicates increased conservation with dark red showing completely conserved positions. Unconserved residues are shown in grey, with dark grey as least conserved. The XIP binding site consists of a conserved surface and a variable surface. Residues of interest are indicated by position and labeled. The inset shows the DBD and TPR domain interface that consists of highly conserved residues, with hydrogen bonds indicated by a dashed green line. (B) The solvent accessible hydrophobic residues of the ComR S. suis surface are highlighted in orange (C) Electrostatic surface potential as calculated by APBS with a contour of -10 kT/e to 10 kT/e. (D) Alignment of ComR S. suis with all species studied in this work. Secondary structure is annotated as Fig 4. Conserved and homologous residues are highlighted in red with the XIP variable face residues in a gray box. The alignment was generated by Clustal Omega and Espript3