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. 2018 Nov 5;150(11):1554–1566. doi: 10.1085/jgp.201812124

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© 2018 Kasimova et al.

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Figure 4. — Two alternative conformations of the S6 helix in the TRPV1 closed and open states. (A) Coupling between N676 and Y671. The top left panel shows Y671 orientation (the cosine of the angle between the Cα-Cγ vector and the pore axis) and the π-bulge position (the difference between the two distances: I672 carbonyl oxygen–N676 amine hydrogen and Y671 carbonyl oxygen–N676 amine hydrogen; positive values indicate the location of the π-bulge on I672, while negative ones indicate that the π-bulge is on Y671). Only two conformations are observed: open state (1), Y671 is perpendicular to the pore axis, and the π-bulge is on I672; and closed state (2), Y671 is parallel to the pore axis, and the π-bulge is on Y671. The bottom left panel shows the distance between N676 carboxamide carbon and I672 carbonyl oxygen and the π-bulge position. The energetically most favorable conformations are open state (1), a hydrogen bond between N676 carboxamide and I672 carbonyl oxygen is present, and the π-bulge is on I672; and closed state (2), the hydrogen bond between N676 carboxamide and I672 carbonyl oxygen is absent, and the π-bulge is on Y671. The right panel shows the cartoon representations of the two conformations. Y672 is colored in purple, the π-bulge in red, and N676 in orange. The dashed lines show the network of hydrogen bonds. (B) A change of Y671 orientation results in a displacement of the pore helix. The top panel shows the conformations of Y671 and of the adjacent pore helix in the open (left) and closed (right) states. The bottom panel shows the superposition between the pore helix in the open (solid) and closed (transparent) states.