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. 2021 Jan 4;4:28. doi: 10.1038/s42003-020-01531-x

Fig. 3. Structural and functional variation of the interconnecting loop.

Fig. 3

a Surface representation of monomeric AtCRY2-PHRtetramer (light blue) and connector region of PHR domain is highlighted in red. Helices are shown as cylinders. b Superposition of connector regions of AtCRY2-PHRtetramer (red) and active mutant ZmCRY1CW368A (blue, PDB: 6LZ3); 0.8 Å r.m.s.d is calculated by PyMOL. c Comparison of connector region of AtCRY2-PHRtetramer (red) with AtCRY1 (green, PDB: 1U3C), AtCRY2-PHRmonomer (yellow, PDB: 6K8I), and AtCRY2-PHRinactive (Magenta, PDB: 6K8K); r.m.s.d of 1.65 Å, 1.49 Å and 1.78 Å, respectively are calculated by PyMOL. d Sidechain view of connector loop region of AtCRY2-PHRtetramer (red) and AtCRY2-PHRmonomer (yellow, PDB: 6K8I). e Sequence alignment and conservation of CRYs interconnecting loop. Residues are colored by traditional amino acid properties in RasMol colors. Arrows indicate residues highlighted in ad.