Publication Abstract from PubMed
Peridinin-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.
Structural basis of light harvesting by carotenoids: peridinin-chlorophyll-protein from Amphidinium carterae.,Hofmann E, Wrench PM, Sharples FP, Hiller RG, Welte W, Diederichs K Science. 1996 Jun 21;272(5269):1788-91. PMID:8650577[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
