1ppr
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1ppr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ppr, resolution 2.0Å" /> '''PERIDININ-CHLOROPHYLL...)
Next diff →
Revision as of 21:53, 20 November 2007
|
PERIDININ-CHLOROPHYLL-PROTEIN OF AMPHIDINIUM CARTERAE
Overview
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.
About this Structure
1PPR is a Single protein structure of sequence from Amphidinium carterae with CLA, PID and DGD as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis of light harvesting by carotenoids: peridinin-chlorophyll-protein from Amphidinium carterae., Hofmann E, Wrench PM, Sharples FP, Hiller RG, Welte W, Diederichs K, Science. 1996 Jun 21;272(5269):1788-91. PMID:8650577
Page seeded by OCA on Wed Nov 21 00:00:28 2007
