Figure 3
The architecture of the GspLfld dimer and the hydrophobic nature of the interaction interface is conserved. (a) Crystal form 1 of GspLfld dimer seen from the side and from the top. The inset reveals the details of the hydrophobic interface. The interacting residues are located on strand β1 and helix α1 and their symmetry related interaction partners. Leu327 is built in the model in two different conformations, labeled a and b in the bottom panel. (b) Side-view of crystal form 2 of the GspLfld dimer. In contrast to crystal form 1, the dimer is present in the asymmetric unit but the interface also involves residues from strand β1 and helix α1 of chain A and strand β1′ and helix α1′ of chain B. In bottom panel, crystal form 2 is shown in surface representation. All atoms are colored according to the type (oxygens: red, nitrogens: blue) and carbon atoms are in the respective chain color. Display of chain B as it would face chain A at the GspLfld dimer interface reveals a buried hydrophobic patch in the GspLfld dimer (inner dotted ellipse). (c) GspLfld dimer from Vibrio parahaemolyticus, PDB: 2w7v21. For details on the conservation of the interacting residues see Figure S2.
