4rmp

Publication Abstract from PubMed

Isolated phycobilisome (PBS) sub-assemblies have been widely subjected to X-ray crystallography analysis to obtain greater insights into the structure-function relationship of this light harvesting complex. Allophycocyanin (APC) is the phycobiliprotein always found in the PBS core complex. Phycocyanobilin (PCB) chromophores, covalently bound to conserved Cys residues of alpha- and beta- subunits of APC, are responsible for solar energy absorption from phycocyanin and for transfer to photosynthetic apparatus. In the known APC structures, heterodimers of alpha- and beta- subunits (known as alphabeta monomers) assemble as trimer or hexamer. We here for the first time report the crystal structure of APC isolated from a marine cyanobacterium (Phormidium sp. A09DM). The crystal structure has been refined against all the observed data to the resolution of 2.51 A to Rwork (Rfree) of 0.158 (0.229) with good stereochemistry of the atomic model. The Phormidium protein exists as a trimer of alphabeta monomers in solution and in crystal lattice. The overall tertiary structures of alpha- and beta- subunits, and trimeric quaternary fold of the Phormidium protein resemble the other known APC structures. Also, configuration and conformation of the two covalently bound PCB chromophores in the marine APC are same as those observed in fresh water cyanobacteria and marine red algae. More hydrophobic residues, however, constitute the environment of the chromophore bound to alpha-subunit of the Phormidium protein, owing mainly to amino acid substitutions in the marine protein.

Crystal Structure of Allophycocyanin from Marine Cyanobacterium Phormidium sp. A09DM.,Sonani RR, Gupta GD, Madamwar D, Kumar V PLoS One. 2015 Apr 29;10(4):e0124580. doi: 10.1371/journal.pone.0124580., eCollection 2015. PMID:25923120^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.