REFINED CRYSTAL-STRUCTURE OF PHYCOERYTHRIN FROM PORPHYRIDIUM-CRUENTUMAT 0.23-NM RESOLUTION AND LOCALIZATION OF THE GAMMA-SUBUNIT

The three-dimensional structure of the light-harvesting pigment-protei n b-phycoerythrin from the red alga Porphyridium cruentum has been det ermined at 0.23-nm resolution. The b-phycoerythrin structure is very s imilar to the structure of B-phycoerythrin from Porphyridium sordidum. Besides three non-identical residues there are only small differences between b-phycoerythrin and B-phycoerythrin alpha and beta subunits, respectively. In the crystals b-phycoerythrin forms an (alphabeta)6 he xamer (molecular mass: 236 kDa), whereas B-phycoerythrin additionally contains a 30-kDa gamma subunit. The comparison of the b-phycoerythrin and B-phycoerythrin electron-density maps clearly reveals, that the g amma subunit is located inside the (alphabeta)6 aggregate.