|
Figure 2.
Fig. 2. Structure of the selectivity filter of the wild-type
EcClC Fab complex. (A) Stereo view of electron density in the
selectivity filter at 2.5 Å, contoured at 1 . The view
is from the dimer interface within the membrane. The cytoplasm
is on the bottom, the extracellular side on the top. The map was
calculated from native amplitudes and solvent-flattened two-fold
averaged phases. The refined protein model is shown as sticks.
An (F[Br] - F[Cl]) difference Fourier map at 2.8 Å,
contoured at 4 , is shown
in red. (B) Stereo view of the ion-binding sites. Selected
residues in the vicinity of the bound chloride ions are shown.
Hydrogen bonds between the protein and chloride ions (red
spheres) as well as between the side chain of Glu148 and the
rest of the protein are shown as black dashed lines.
|