Figure 5From: Crystal structures of an Extracytoplasmic Solute Receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for α-keto acid bindingA conserved dimeric interface. A: The structure of one monomer is represented as a surface that is colored according to the sequence conservation pattern generated using 100 homologous sequences and as found by ConSurf [42]. B: Weblogo representation of the terminal swapped helix using the same set of sequences. In this representation the overall height of a stack indicates the sequence conservation at that position, while the height of symbols within the stack indicates the relative frequency of each amino acid at that position.Back to article page