Fig. 2: Overview of the structure of KimA.
From: Structural basis of proton-coupled potassium transport in the KUP family
a KimA dimer viewed from the membrane, with one monomer coloured in grey and the other in a rainbow, from blue (N terminus) to red (C terminus). b Schematic representation of the topology of KimA. Each KimA monomer is composed of 12 TM helices, organized in a 5 + 5 inverted structural repeat and two additional, C-terminal TM helices located at the periphery of the dimer. The last TM helix extends into the cytoplasm and positions the soluble domain below the TM domain of the second monomer. c The cytoplasmic domain of a KimA monomer is formed by a parallel, five-stranded β-sheet sandwiched by four α-helices, forming a continuous 10-stranded β-sheet in the dimer. d Side view and e top view of the membrane domain of a KimA monomer.
