Fig. 2: Conformational difference on the luminal side. | Nature Communications

Fig. 2: Conformational difference on the luminal side.

From: Molecular mechanism underlying regulation of Arabidopsis CLCa transporter by nucleotides and phospholipids

Fig. 2

a Comparison of AtCLCa-Cl− (blue) and AtCLCa-NO3− (golden). The AtCLCa-NO3− protomer was superimposed onto one protomer of AtCLCa-Cl− dimer. The αI–J loop is colored green in AtCLCa-Cl− and red in AtCLCa-NO3−. b Comparison of the AtCLCa-Cl− and AtCLCa-NO3− protomer. The CBS domains are hidden for clearance. The dashed circle indicates segments of αI–J loop near the outlet of ion transport pathway in the luminal side. The side chain of gating glutamate Glu203 is shown as spheres. c, d Electrostatic potential surface of the AtCLCa-Cl− (c) and AtCLCa-NO3− (d) protomer. The dashed circle indicates the outlet of ion transport pathway in luminal side.

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