Fig. 5
From: Structural snapshot of a bacterial phytochrome in its functional intermediate state
Crystal packing details of Agp2-PAiRFP2 monomers in the asymmetric unit. Surface representation of Agp2-PAiRFP2 (PDB entry 6G20) Mol A and B per asymmetric unit in the Meta-F sub-states. a (PAS, GAF, PHY in grey, yellow, blue, respectively; N-terminus highlighted in red) shows the free N-terminus for molecule A (Mol A), whereas the N-terminus of molecule B (Mol B) is packed against the PAS domain of Mol A. Owing to the higher flexibility, the N-terminus of Mol A can undergo a β-facial to α-facial orientation transition of the BV-binding Cys13 in the Meta-F state. b Close-up view into the packed N-terminal region of Mol B dimer shown as surface and cartoon representation. c Cartoon representation of the dimer interface of Mol A and B, including the N-terminus of Mol B with the β-facial orientation of Cys13. Amino acids involved in the interface are highlighted as sticks. Compared to Mol A (Fig. 7d, e), some amino acids in Mol B display a positional heterogeneity as reflected by the alternate conformations of Tyr165 and Phe192
