Structural basis of light harvesting by carotenoids: Peridinin-chlorophyll-protein from Amphidinium carterae
Structural basis of light harvesting by carotenoids: Peridinin-chlorophyll-protein from Amphidinium carterae
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DOI：
10.1126/science.272.5269.1788
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发表时间：
1996-06-21
期刊：
影响因子：
56.9
通讯作者：
Diederichs, K
中科院分区：
文献类型：
--
作者：
Hofmann, E;Wrench, PM;Diederichs, K
Peridin-chlorophyll-protein是一种水溶性的捕光复合物，具有蓝绿色吸收的类胡萝卜素作为其主要色素，存在于大多数光合甲藻中，其高分辨率（2.0埃）X-射线结构揭示了一种非晶体学三聚体，其中每种多肽含有α-螺旋氨基和羧基末端结构域的不寻常的卷曲折叠，这些结构域构成具有伪双重对称性的支架，其围绕由两个脂质、八个多甲藻素和两个叶绿素a分子填充的疏水空腔，从多甲藻素到叶绿素的有效激子能量转移的结构基础是在货车的叶绿素周围的多甲藻素簇中发现的der Waals距离
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.