1ppr
From Proteopedia
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|PDB= 1ppr |SIZE=350|CAPTION= <scene name='initialview01'>1ppr</scene>, resolution 2.0Å | |PDB= 1ppr |SIZE=350|CAPTION= <scene name='initialview01'>1ppr</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=DGD:DIGALACTOSYL+DIACYL+GLYCEROL+(DGDG)'>DGD</scene>, <scene name='pdbligand=PID:PERIDININ'>PID</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ppr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ppr OCA], [http://www.ebi.ac.uk/pdbsum/1ppr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ppr RCSB]</span> | ||
}} | }} | ||
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[[Category: Hofmann, E.]] | [[Category: Hofmann, E.]] | ||
[[Category: Welte, W.]] | [[Category: Welte, W.]] | ||
| - | [[Category: CLA]] | ||
| - | [[Category: DGD]] | ||
| - | [[Category: PID]] | ||
[[Category: carotenoid]] | [[Category: carotenoid]] | ||
[[Category: dinoflagellate]] | [[Category: dinoflagellate]] | ||
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[[Category: photosynthesis]] | [[Category: photosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:02:55 2008'' |
Revision as of 20:02, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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