Extended Data Fig. 5: Two interfaces and schematic representation of interactions in the tetramer.
From: Structural insights into the photoactivation of Arabidopsis CRY2
a, Two interfaces of tetramer. CRY2 tetramer is comprised of mol A, B, C, and D that are shown as light pink, cyan, light blue, and yellow, respectively. Connector regions are colored in magenta, red, blue, and green, respectively. Red and black squares show close-up views of interface 1 and interface 2 with 90° rotations, respectively. Numbered helices are involved in the tetramerization. b, Schematic representation of CRY2 tetramer interactions. Extensive interaction networks of interface 1 and interface 2. Residues in mol A, mol B, and mol C involved in interactions are indicated by purple, dark green, and light blue rectangles, respectively. In interface 1, E18 in helix α1; H62 and S66 in helix α3; D160 in helix α6; M167 and R173 in the loop of the connector region; N222 in helix α8; and M267 and R274 in helix α11 from mol A coordinate with M267, R274, R173, M167, D160, N222, E18, H62, and S66 from mol B via hydrogen bonds, respectively (left panel black dashed lines). I17, L159, I163, W172, W214, F262, M267, I270, and I271 interact with each other via hydrophobic interactions (left panel black solid line). Interface 2 is mainly mediated by a dozen hydrogen bonds formed by R50, S202, K329, Q333, R346, W349, E436, R439, A458, and E462 from the two protomers.
