Fremyella diplosiphon

Fig. 12. Amino acid sequence of the three biliproteins from the phycobilisome of the cyanobacterium M. laminosus (Fischerella PCC 7603) a/3-APC, a/3-C-PC, a/3-PEC and of C-PE from the cyanobacterium Fremyella diplosiphon (Calothrix UTEX 481). [PEB] is the phycoerythrobilin chromophore of C-PE the PCB-chromophores of a/8-APC, a/3-C-PC and -PEC and the PXB-chromophore of a-PEC are bound at homologous positions (to Cys and to Cys" ) and are not shown. The names of the amino acids are abbreviated according to the one-letter code (Eur. J. Biochem. (1983) 183, 9-33).

Fig, 13. Three-dimensional structure of C-phycocyanin (C-PC) o-subunit and j8-subunit (A and B) and o/3-trimer (C) derived from X-ray diffraction analysis of crystals of C-PC isolated from the cyanobacterium Mastigocladus laminosus (Fischerella PCC 7603) (101,145]. The possible positions of the additional PEB chromophores in C-PE from Fremyella diplosiphon (Calothrix UTEX 481) are adapted to the models of C-PC, using data from the amino acid sequence of C-PE [115]. Positions of the PEB chromophores at cysteine 50/61 X-X and 143a X. The beginning of the insertion 141a-o in J-C-PE is indicated by an arrow (— ). 

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