1ppr: Difference between revisions

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[[Image:1ppr.gif|left|200px]]
{{Seed}}
[[Image:1ppr.png|left|200px]]


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{{STRUCTURE_1ppr|  PDB=1ppr  |  SCENE=  }}  
{{STRUCTURE_1ppr|  PDB=1ppr  |  SCENE=  }}  


'''PERIDININ-CHLOROPHYLL-PROTEIN OF AMPHIDINIUM CARTERAE'''
===PERIDININ-CHLOROPHYLL-PROTEIN OF AMPHIDINIUM CARTERAE===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_8650577}}, adds the Publication Abstract to the page
(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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