Abstract
Peridinin-Chlorophyll a-Protein (PCP) is a water-soluble, yet membrane-attached photosynthetic light-harvesting complex believed to reside in the interior of the thylakoid. We have recently reported the x-ray crystallographic structure of PCP from the dinoflagellate Amphidinium carterae, which crystallizes as a trimer [1]. Overall, the PCP polypeptide (312 amino acid residues) has the shape of the hull of a ship enclosing a cargo of two lipids, two chlorophyll a and eight carotenoid molecules. Each monomer is composed of a pseudosymmetry-related N- and C-terminal half of eight helices each adopting a peculiar topology whose relation to the globin-like fold is explored in this presentation. Based on the resemblance of folds and available data on myoglobin folding, we discuss a possible folding pathway for the PCP holoprotein which has to assemble during and after passage of the apoprotein through the thylakoid membrane.
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Diederichs, K., Hofmann, E. (1998). Structural Relation of Peridinin-Chlorophyll A-Protein (PCP) and Proteins with Globin-Like Fold. In: Ens, W., Standing, K.G., Chernushevich, I.V. (eds) New Methods for the Study of Biomolecular Complexes. NATO ASI Series, vol 510. Springer, Dordrecht. https://doi.org/10.1007/978-94-015-9046-4_21
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DOI: https://doi.org/10.1007/978-94-015-9046-4_21
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