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. 2019 May 9;8:e47746. doi: 10.7554/eLife.47746

Figure 2. Rearrangements of the cytoplasmic domains in the TRPV3K169A structure.

(A) The cytoplasmic inter-protomer interface in TRPV3WT (left panel) and TRPV3K169A (right panel). The CTD and the putative N-terminal region are highlighted in red and purple, respectively. (B) Close-up view of the rearrangements in the cytoplasmic domains. In the TRPV3WT, the distal CTD (highlighted in red) coils around the βCD (highlighted in grey) (left panel). In the TRPV3K169A structure, the distal CTD undergoes a coil-to-helix transition (highlighted in red). An additional polypeptide density (highlighted in purple) is observed near the front of the βCD (highlighted in grey) and the proximal CTD, in the vicinity of the space occupied by the distal CTD coil in TRPV3WT and was assigned as a putative N-terminal domain from the neighboring protomer (NTD−1).

Figure 2.

Figure 2—figure supplement 1. Cryo-EM data collection and processing, TRPV3K169A.

Figure 2—figure supplement 1.

(A) A representative micrograph from the TRPV3K169A data collection. (B) 3D reconstruction workflow. (C) Euler distribution plot. Red regions show the best represented views. (D) Local resolution estimate, calculated in Relion. (E) FSC curves calculated between the half maps (blue), atomic model and the full map (red) and between the model and each half-map (orange and green).
Figure 2—figure supplement 2. Electron density in the TRPV3K169A cryo-EM map.

Figure 2—figure supplement 2.

(A) Representative electron densities in the TRPV3K169A cryo-EM map. Densities are contoured at level 0.015 and radius 2. (B–C) Connectivity between the ARD and the putative N-terminal region. The unsharpened TRPV3K169A map is contoured at level 0.006.