Fig. 2: CTD dimerization interface of SOS1. | Nature Communications

Fig. 2: CTD dimerization interface of SOS1.

From: Architecture and autoinhibitory mechanism of the plasma membrane Na+/H+ antiporter SOS1 in Arabidopsis

Fig. 2

a Overall structure of the SOS1 dimer model. Helices involved in the dimeric interactions are highlighted. Three regions in the dimeric CTD are boxed. b, c Interactions between HC1 and HC2 from one protomer and HC7′ from another protomer viewed from the front of the structure (b), and from the left (c). Sidechains of residues contributing to dimerization are shown as sticks. The hydrogen bond between E470 and Y691′ is shown as dashed lines. d Electrostatic complementary interactions between the HC1-HC2 loop and the pocket formed by α-CTD′ and CNBLD′ from another subunit. The positively charged pocket is shown according to its electrostatic potential calculated with the Adaptive Poisson-Boltzmann Solver (APBS) plugin in Pymol and contoured at ±5 kT/e. Residues that are harbored in the pocket and involved in the interactions are shown as sticks. e Electrostatic complementary interactions between the juxtamembrane helix HC8′ and TM5, TM6 of TMD and HC1 of α-CTD from the other subunit. Hydrogen and salt-bridge bonds are shown as dashed lines.

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