Fig. 4: Structural modeling of the OPNR complex formed by OPNR, OAP1, OAP2, CDC48D, and CIP111. | Nature Communications

Fig. 4: Structural modeling of the OPNR complex formed by OPNR, OAP1, OAP2, CDC48D, and CIP111.

From: Ribosome biogenesis in plants requires the nuclear envelope and mitochondria localized OPENER complex

Fig. 4

A The purified recombinant proteins His-OAP1, OAP2 and OPNR before (lane 1) and after (lane 2) His-tag removal. The molar ratio measured for OAP1: OAP2: OPNR was 1.2: 1: 1.1. B–F: AlphaFold predicted structures of the OPNR-OAP1-OAP2 trimer (B), the interaction between OPNR-OAP1-OAP2 trimer and CIP111 (C), the interaction between OPNR-OAP1-OAP2 trimer and CDC48D (D), the interaction between OPNR-OAP1-OAP2 trimer and the N-terminus of CIP111 (E), and the interaction between OPNR-OAP1-OAP2 trimer, CIP111 and CDC48D (F). In each Fig., the three-dimensional structure is shown from two different angles. The predicted template modelling (pTM) score and the interface predicted template modelling (ipTM) score is shown for each prediction. The predicted aligned error (PAE) plots provided for each predicted structure demonstrate the high confidence (dark green) and low confidence (pale green) regions for the predicted structure. The colour coding indicates the protein identity as shown in the PAE plots. The N-terminus domain of CIP111 (N) and the two ATPase domains (D1 and D2) of CIP111 and CDC48D were labelled.

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