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pubmed-article:8650577pubmed:abstractTextPeridinin-chlorophyll-protein, a water-soluble light-harvesting complex that has a blue-green absorbing carotenoid as its main pigment, is present in most photosynthetic dinoflagellates. Its high-resolution (2.0 angstrom) x-ray structure reveals a noncrystallographic trimer in which each polypeptide contains an unusual jellyroll fold of the alpha-helical amino- and carboxyl-terminal domains. These domains constitute a scaffold with pseudo-twofold symmetry surrounding a hydrophobic cavity filled by two lipid, eight peridinin, and two chlorophyll a molecules. The structural basis for efficient excitonic energy transfer from peridinin to chlorophyll is found in the clustering of peridinins around the chlorophylls at van der Waals distances.lld:pubmed
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pubmed-article:8650577pubmed:articleTitleStructural basis of light harvesting by carotenoids: peridinin-chlorophyll-protein from Amphidinium carterae.lld:pubmed
pubmed-article:8650577pubmed:affiliationFakultät für Biologie, Universität Konstanz, Germany.lld:pubmed
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