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. 2022 Nov 3;119(45):e2207067119. doi: 10.1073/pnas.2207067119

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Copyright © 2022 the Author(s). Published by PNAS.

This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND).

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Fig. 7. — Structural comparisons of KCNQ1-CaM_ML277-PIP2-A and KCNQ1-CaM_ML277-PIP2-B. (A) Different structure arrangements of CTD and CaM in KCNQ1-CaM_ML277-PIP2-A and KCNQ1-CaM_ML277-PIP2-B. S6, S6-HA linker, HA, HB, and HC helices of KCNQ1 are colored in marine, red, cyan, green, and yellow, respectively. The N-lobe and C-lobe of CaM are shown in wheat and pink, respectively. (B) Structural comparison of one KCNQ1 subunit in KCNQ1-CaM_ML277-PIP2-A (blue) and KCNQ1-CaM_ML277-PIP2-B (green) in two side views. The S6-HA linker ‘‘KHFN’’ motif that undergoes structural rearrangement from a loop to a helix is colored in red. (C) Structural comparison of the HA, HB, and HC helices in KCNQ1-CaM_ML277-PIP2-A (blue) and KCNQ1-CaM_ML277-PIP2-B (green) in the top view with TMD and HA/HB from the other three subunits omitted for clarity. The N-terminal residue Val538 of HC rotates by ∼97° from KCNQ1-CaM_ML277-PIP2-A to KCNQ1-CaM_ML277-PIP2-B. (D) The binding of PIP₂ induces a 1–2 Å movement of the S2-S3 linker in KCNQ1-CaM_ML277-PIP2-B (green) in comparison with that in KCNQ1-CaM_ML277-PIP2-A (blue). The PIP₂ in KCNQ1-CaM_ML277-PIP2-A is not shown for clarity. (E) Interactions between S6 and HB-HC linker. The dashed lines indicate the salt bridge Arg360-Asp537 and the hydrogen bonds Gln359-Tyr536 and His363-Lys534.