1ppr_peridinin_chlorophyll_protein_trimer.png
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Summary
Description 1ppr peridinin chlorophyll protein trimer.png |
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. |
Date | |
Source | Own work |
Author | Opabinia regalis |
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