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. 2012 May 30;7(5):e38187. doi: 10.1371/journal.pone.0038187

Figure 1. Schematic representation of domain composition in ArcB and coiled coil.

Figure 1

prediction. A) The ArcB sensor kinase is attached to the plasma membrane by TM1 corresponding to residues 23 to 41 and TM2 corresponding to residues 58 to 77. The linker region contains a coiled coil motif with a putative leucine-zipper (gray filled block) and two redox-active cysteine residues 180 and 241. The primary transmitter domain (H1) contains the conserved His292 and the catalytic determinants N, G1, and G2. The G1 and G2 sequences typify nucleotide-binding motifs. The receiver domain (D1) contains the conserved Asp576, and the histidine phosphotransfer domain (Hpt/H2) contains the conserved His717. Adapted from [7] but with some modifications. B) Prediction of coiled coil motifs along the ArcB amino acid sequence. Above is plotted the probability of coiled coil structure occurrence along the ArcB sequence, as predicted by the COILS/PCOILS tool. Below is presented the sequence of the ArcB coiled-coil motif with its heptad repeats, and the leucine zipper as predicted by the program 2ZIP. C) Model of the ArcB coiled coil section covering residues 73–121. The structure prediction was generated based on the crystal structure of a model dimeric coiled coil (PDB code 3he5). The positions of leucine residues 73, 80, 87, 94, 108 and 115 are indicated in yellow and the position of Leu 102, which was used as an experimental control, is shown in blue.