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Science 21 June 1996:
Vol. 272. no. 5269, pp. 1788 - 1791
DOI: 10.1126/science.272.5269.1788
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Reports

Structural Basis of Light Harvesting by Carotenoids: Peridinin-Chlorophyll-Protein from Amphidinium carterae

Eckhard Hofmann, Pamela M. Wrench, Frank P. Sharples, Roger G. Hiller, Wolfram Welte, * Kay Diederichs

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.

E. Hofmann, W. Welte, K. Diederichs, Fakultät für Biologie, Universität Konstanz, Postfach 5560 (M656) , 78434 Konstanz, Germany.
P. M. Wrench, F. P. Sharples, R. G. Hiller, School of Biological Sciences, Macquarie University, New South Wales 2109, Australia.
* To whom correspondence should be addressed. E-mail: Wolfram.Welte{at}uni-konstanz.de


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