Extended Data Fig. 7: Mutational analysis of BIC2-CRY2N interface.
From: Structural insights into BIC-mediated inactivation of Arabidopsis cryptochrome 2
a, Extensive interaction networks between BIC2 and CRY2N. Residues of BIC2 and CRY2N involved in interactions are shown in yellow and cyan rectangles, respectively. Black outlines indicate residues that were mutated to verify the interactions in the BIC2-CRY2N structure. b, Analysis of the interactions between wild type BIC2 with CRY2 mutants (labeled with asterisk). c, Interactions analysis of BIC2 mutants (labeled with asterisk) with wild type CRY2. For BIC2, we mutated residues that interact with CRY2 via their side chains (residues labeled with magenta dots in Extended Data Fig. 7d). For CRY2, there are 36 residues involved in BIC interactions. PDB 6K8K was loaded to PDBePISA (https://www.ebi.ac.uk/pdbe/pisa/) to analyze the interface of BIC2 and CRY2N. We then mutated 16 residues with the highest accessible surface area (ASA) and buried surface area (BSA). Residues that have a higher buried area percentage in PDBePISA interface analysis may make greater contributions to the interaction. Residues critical for complex formation are shown on a gray background. d, Sequence alignment of CID domains17 of BICs from different plant species. Secondary structural elements of BIC2 are shown above the sequence. The alignment was performed using MultAlin and ENDscript programs. Amino acid residue numbers are indicated to the left and right of each sequence. Sequence identity is indicated in white letters on a red background. Cyan and magenta dots represent the BIC2 residues interacting with CRY2N via main chains or side chains, respectively. The latter BIC2 residues were mutated to verify the interactions. Uncropped gel images of panels b and c are available as source data.
