Structural basis of light harvesting by carotenoids: peridinin-chlorophyll-protein from Amphidinium carterae.
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.
Hofmann
E
E
Fakultät für Biologie, Universität Konstanz, Germany.
Wrench
P M
PM
Sharples
F P
FP
Hiller
R G
RG
Welte
W
W
Diederichs
K
K
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*
D015800:Protozoan Proteins; C073227:peridinin chlorophyll-a protein, Dinophyceae; D002734:Chlorophyll; C016040:peridinin; D002338:Carotenoids; D000077194:Chlorophyll A