Stereo representation of the interaction between
the linker polypeptide and monomer 2. The Cα-aligned
structures are shown for the symmetric, linker-free allophycocyanin
(blue), monomer 3, which has no interaction with the linker polypeptide
(red), and monomer 2 (yellow), which interacts with the N terminus of
the long linker α-helix (orange). Water molecules are omitted for
clarity. Phe-37 of the linker inserts between Tyr-87 and the pyrrole
ring B of the corresponding β-subunit displacing both to opposite
directions and disrupting the stacking interaction between the two
aromatic ring systems, which is seen at the other two β-chromophores
of the linker containing trimer. This figure was prepared in
main (29).