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Summary
| Description |
English: Crystal structure of the soluble peridinin-chlorophyll-protein complex from the photosynthetic dinoflagellate Amphidinium carterae, showing the noncrystallographic trimer consistent with biochemical observations about the natural oligomer state. This complex is found in many photosynthetic dinoflagellates and involves a boat or cradle-shaped protein with two pseudosymmetrical repeats of eight alpha helices (shown in the lower left monomer in blue and orange) wrapped around a pigment-filled central cavity. Each eight-helix segment binds one chlorophyll molecule (green, with central magnesium ion shown as a green sphere), one diacylglycerol molecule (yellow) and four peridinin molecules (gray). For the other two monomers, only the protein is shown, in tan and red. Compare File:1ppr peridinin chlorophyll protein.png, which shows only the lower left monomer in a similar orientation.
Rendered using PyMol from PDB ID 1PPR. Hofmann E, Wrench PM, Sharples FP, Hiller RG, Welte W, Diederichs K. Structural basis of light harvesting by carotenoids: peridinin-chlorophyll-protein from Amphidinium carterae. Science. 1996;272(5269):1788-91. DOI 10.1126/science.272.5269.1788. |
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| Source | Own work |
| Author | Opabinia regalis |
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
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| current | 20:59, 14 October 2016 | | 2,048 × 2,048 (2.59 MB) | Opabinia regalis | {{Information |Description ={{en|1=Crystal structure of the soluble peridinin-chlorophyll-protein complex from the photosynthetic dinoflagellate ''Amphidinium carterae'', showing the noncrystallographic trimer consistent with biochemical observation... |
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