1PPR

PERIDININ-CHLOROPHYLL-PROTEIN OF AMPHIDINIUM CARTERAE

Summary for 1PPR

• Entry DOI: 10.2210/pdb1ppr/pdb
• Descriptor: PERIDININ-CHLOROPHYLL PROTEIN, CHLOROPHYLL A, PERIDININ, ... (5 entities in total)
• Functional Keywords: light harvesting protein, photosynthesis, carotenoids, dinoflagellates, light-harvesting protein
• Biological source: Amphidinium carterae
• Cellular location: Plastid, chloroplast: P80484
• Total number of polymer chains: 3
• Total formula weight: 123801.37

Authors

Hofmann, E.,Welte, W.,Diederichs, K. (deposition date: 1996-03-06, release date: 1997-08-20, Last modification date: 2024-02-14)

Primary citation

Hofmann, E.,Wrench, P.M.,Sharples, F.P.,Hiller, R.G.,Welte, W.,Diederichs, K.
Structural basis of light harvesting by carotenoids: peridinin-chlorophyll-protein from Amphidinium carterae.
Science, 272:1788-1791, 1996

PubMed 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.

PubMed: 8650577

Experimental method

X-RAY DIFFRACTION (2 Å)