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1ppr

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[[Image:1ppr.gif|left|200px]]
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{{STRUCTURE_1ppr| PDB=1ppr | SCENE= }}
{{STRUCTURE_1ppr| PDB=1ppr | SCENE= }}
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'''PERIDININ-CHLOROPHYLL-PROTEIN OF AMPHIDINIUM CARTERAE'''
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===PERIDININ-CHLOROPHYLL-PROTEIN OF AMPHIDINIUM CARTERAE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8650577 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8650577}}
==About this Structure==
==About this Structure==
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[[Category: Light harvesting protein]]
[[Category: Light harvesting protein]]
[[Category: Photosynthesis]]
[[Category: Photosynthesis]]
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Revision as of 18:36, 28 July 2008

Image:1ppr.png

Template:STRUCTURE 1ppr

PERIDININ-CHLOROPHYLL-PROTEIN OF AMPHIDINIUM CARTERAE

Template:ABSTRACT PUBMED 8650577

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

Page seeded by OCA on Mon Jul 28 21:36:20 2008

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