Structural basis of light harvesting by carotenoids: peridinin-chlorophyll-protein from Amphidinium carterae
| Autor: | Eckhard Hofmann, Kay Diederichs, Pamela M. Wrench, Frank P. Sharples, Roger G. Hiller, Wolfram Welte |
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| Rok vydání: | 1996 |
| Předmět: |
Chlorophyll
Models Molecular Chlorophyll a Protein Folding Stereochemistry Protein Conformation ved/biology.organism_classification_rank.species Molecular Conformation Protozoan Proteins Trimer Photosynthetic pigment Biology Photosynthesis Crystallography X-Ray Protein Structure Secondary chemistry.chemical_compound symbols.namesake Amphidinium carterae ddc:570 Animals Multidisciplinary ved/biology Chlorophyll A Hydrogen Bonding Carotenoids Peridinin chemistry Energy Transfer symbols Dinoflagellida van der Waals force |
| Zdroj: | Science (New York, N.Y.). 272(5269) |
| ISSN: | 0036-8075 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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