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. 2022 Sep 12;298(10):102482. doi: 10.1016/j.jbc.2022.102482

Table 1.

Structural data and models available for SMR transporters Gdx-Clo and EmrE

Protein Substrate Method (max. resolution) PDB Reference
EmrE Tetraphenylphosphonium (TPP+) Electron microscopy with 2D crystals (7.5 Å) Data: EMD-1087
Model: 2I68
Data (12)
Model (58)
Gdx-Clo Gdm+ Crystallography (3.50 Å) 6WK5 (4)
Gdx-Clo PhenylGdm+ Crystallography (2.53 Å) 6WK8 (4)
Gdx-Clo OctylGdm+ Crystallography (2.32 Å) 6WK9 (4)
Gdx-Clo None (pH 5.0) Crystallography (2.32 Å) 7SZT (3)
aEmrE3 None (pH 5.2) Crystallography (2.85 Å) 7MH6 (3)
aEmrE3 Methyl viologen Crystallography (3.13 Å) 7MGX (3)
aEmrE3 TPP+ Crystallography (3.36 Å) 7SV9 (3)
aEmrE3 Methyltriphenylphosphonium Crystallography (3.22 Å) 7SSU (3)
aEmrE3 Benzyltrimethylammonium Crystallography (3.91 Å) 7T00 (3)
aEmrE3 Harmane Crystallography (3.91 Å) 7SVX (3)
bEmrE S64V Tetra(4-fluorophenyl) phosphonium/pH 5.8 NMR 7JK8 (80)
bEmrE S64V Tetra(4-fluorophenyl) phosphonium/pH 8.0 NMR 7SFQ (81)

Abbreviation PDB, Protein Data Bank.

a

The construct EmrE3 bears three functionally neutral mutations, E25N, W31I, and V34M, to facilitate crystal formation (3).

b

The S64V mutation preserves substrate binding but reduces the rate of conformational change by 8-fold (88).