Fig. 6: Mechanism of the transmembrane signal transduction.
From: Molecular basis for the phosphorylation of bacterial tyrosine kinase Wzc
a The \({{{{\rm{\theta }}}}}_{{{{\rm{TMH}}}}1},\,{{{{\rm{\theta }}}}}_{{{{\rm{TMH}}}}2},\,{{{{\rm{\theta }}}}}_{{{{\rm{\alpha }}}}1}\) angles are defined as the angles relative to the axis normal to the membrane, and \({{{{\rm{\theta }}}}}_{{{{\rm{TMH}}}}1-{{{\rm{TMH}}}}2}\) is the angle between TMH1 and TMH2. b Boxplot of the metrics for each system. The boxplots represent the variation of the angles over time and the replicates (n = 1500 MD simulations frames. The box bounds the interquartile range divided by the median, with the whiskers extending to a maximum of 1.5 times the interquartile range beyond the box). c Superposition (using the kinase domain) of the initial (white) and final frames (coloured) reveals structural shifts for each state of Wzc. d Time trace of the minimum distance between the residues D28 and K701. e Close up view showing the changes in the interactions between K701 and D28. See Supplementary Table 2 for the summary of the MD simulations. Source data are provided as a Source Data file. f Immunoblot (anti-K30 CPS) of whole cell lysates separated by SDS-PAGE. The wildtype E. coli strain E69 (serotype O9a:H12:K30) was used as a positive control, and E. coli strain CWG285 (Δwzc) was used as a negative control. WT, D28A, K701A, D28A/K701A represent plasmids encoding wild-type Wzc, Wzc with the D28A mutation, Wzc with the K701A mutations, and Wzc with the D28A/K701A mutations respectively. As CPS does not migrate strictly according to size, protein standard is not useful to indicate the molecular weight. These data are representative of three biological replicates.
