Fig. 2: Molecular contacts between PhLP2A and open TRiC chamber. | Nature Communications

Fig. 2: Molecular contacts between PhLP2A and open TRiC chamber.

From: A structural vista of phosducin-like PhLP2A-chaperonin TRiC cooperation during the ATP-driven folding cycle

Fig. 2

a Detailed interaction between PhLP2A and TRiC. (i-ii) Zoomed-in view of the binding between PhLP2A H3 and the apical domain of CCT3 or CCT4 based on AlphaFold prediction. H9 and H10 of each CCT subunit are major interaction sites; their binding modes are similar either on the topological or sequence level. (iii) Interaction between the lower part of TXD and the nucleotide-sensing loop of CCT1. (iv) Helix-to-helix interaction between PhLP2A CTD and CCT6. (v) Helix wheel diagram on PhLP2A CTD-CCT6 showing the amphipathic nature of the helix. b Electrostatic surface charge of PhLP2A and open TRiC chamber. PhLP2A, the top view of TRiC, and unwrap view of the CCT4/1/3/6 half-hemisphere are displayed. Binding sites between PhLP2A and TRiC are indicated with color-coded lines and triangles (dodger blue for the NTD and dark magenta for CTD of PhLP2A). The red circle indicates the TXD binding site to TRiC. Selected views focus on the part of the apical domain where H3 of PhLP2A binds via electrostatic charge interaction. c Surface hydrophobicity of PhLP2A and the open TRiC chamber. Interactions between PhLP2A and TRiC are as indicated in b. While other binding sites are mainly hydrophilic, the TXD binding interface between CCT1/3 and the CTD binding crevasse between CTD3/6 are hydrophobic.

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