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      Refined crystal structure of phycoerythrin from Porphyridium cruentum at 0.23-nm resolution and localization of the gamma subunit.

      European journal of biochemistry / FEBS
      Crystallography, X-Ray, Phycoerythrin, chemistry, isolation & purification, Protein Conformation, Rhodophyta

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          Abstract

          The three-dimensional structure of the light-harvesting pigment-protein b-phycoerythrin from the red alga Porphyridium cruentum has been determined at 0.23-nm resolution. The b-phycoerythrin structure is very similar 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 (alpha beta)6 hexamer (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 gamma subunit is located inside the (alpha beta)6 aggregate.

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          Author and article information

          Journal
          8243457
          10.1111/j.1432-1033.1993.tb18356.x

          Chemistry
          Crystallography, X-Ray,Phycoerythrin,chemistry,isolation & purification,Protein Conformation,Rhodophyta

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