Structural basis of light harvesting by carotenoids: Peridinin-chlorophyll-protein from Amphidinium carterae

被引:377
作者
Hofmann, E
Wrench, PM
Sharples, FP
Hiller, RG
Welte, W
Diederichs, K
机构
[1] UNIV KONSTANZ,FAK BIOL,D-78434 CONSTANCE,GERMANY
[2] MACQUARIE UNIV,SCH BIOL SCI,N RYDE,NSW 2109,AUSTRALIA
关键词
D O I
10.1126/science.272.5269.1788
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:1788 / 1791
页数:4
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