1PPR: Peridinin-chlorophyll-protein of Amphidinium Carterae

Citation:
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.
PDB ID: 1PPRDownload
MMDB ID: 6298
PDB Deposition Date: 1996/3/6
Updated in MMDB: 1998/11
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 1PPR: trimeric; determined by author
Molecular Components in 1PPR
Label Count Molecule
Proteins (3 molecules)
3
Peridinin-chlorophyll Protein
Molecule annotation
Chemicals (36 molecules)
1
6
2
24
3
6
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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