Fig. 1: High-resolution structure of KtrAB in its intact KtrB2A8 assembly compared to the nonphysiological KtrB2A8B2 assembly. | Nature Communications

Fig. 1: High-resolution structure of KtrAB in its intact KtrB2A8 assembly compared to the nonphysiological KtrB2A8B2 assembly.

From: A short intrinsically disordered region at KtrB’s N-terminus facilitates allosteric regulation of K+ channel KtrAB

Fig. 1: High-resolution structure of KtrAB in its intact KtrB2A8 assembly compared to the nonphysiological KtrB2A8B2 assembly.The alternative text for this image may have been generated using AI.

Cryo-EM density maps of a KtrB2A8 with an overall resolution of 2.8 Å and b KtrAB in the nonphysiological KtrB2A8B2 assembly with an overall resolution of 2.5 Å. c Side-view and d bottom-view of the overlay of both structures (KtrB2A8B2 colored, KtrB2A8 pink). The assembly of an additional KtrB dimer to the free side of KtrA does not change the overall structure of the KtrAB complex. Small rotations were identified in two KtrA subunits where the extra KtrB dimer binds, with no significant consequence on the remaining protein. KtrB: gray, D1M2 helix: goldenrod, intramembrane loop: dark cyan, R427: magenta, N-terminus of KtrB: green, KtrA: blue (navy blue, cornflower blue), ADP: orange. If not stated otherwise, coloring is maintained in all figures.

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