title: Structural basis of light harvesting by carotenoids: peridinin-chlorophyll-protein from Amphidinium carterae.
abstract: 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.
authors.affiliation: Fakultät für Biologie, Universität Konstanz, Germany.
authors.forename: E
authors.initials: E
authors.lastname: Hofmann
authors.forename: P M
authors.initials: PM
authors.lastname: Wrench
authors.forename: F P
authors.initials: FP
authors.lastname: Sharples
authors.forename: R G
authors.initials: RG
authors.lastname: Hiller
authors.forename: W
authors.initials: W
authors.lastname: Welte
authors.forename: K
authors.initials: K
authors.lastname: Diederichs
mesh_terms: D000818:Animals; D002338:Carotenoids / Q000737:chemistry*; D002734:Chlorophyll / Q000737:chemistry; D000077194:Chlorophyll A; D018360:Crystallography, X-Ray; D004141:Dinoflagellida / Q000737:chemistry* / Q000378:metabolism; D004735:Energy Transfer; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008968:Molecular Conformation; D010788:Photosynthesis; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D015800:Protozoan Proteins / Q000737:chemistry*
chemical_list: D015800:Protozoan Proteins; C073227:peridinin chlorophyll-a protein, Dinophyceae; D002734:Chlorophyll; C016040:peridinin; D002338:Carotenoids; D000077194:Chlorophyll A