Fig. 4: X-ray structures of barium-bound WT and E71V KcsA.
From: A distinct mechanism of C-type inactivation in the Kv-like KcsA mutant E71V
a Closed-gate and b open-gate structures of WT KcsA with Ba2+ bound at the S4 position of the selectivity filter. The filter is sharply constricted at the level of G77 in both the closed-gate and in the open-gate structures. c Closed-gate and d open-gate structures of E71V KcsA with Ba2+ bound at the S3 position of the selectivity filter. The filter is conductive in the closed-gate structure and narrows in the open-gate structure. Cα-Cα distances between like-residues in opposing protomers are indicated.
