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类胡萝卜素捕光的结构基础:来自卡氏前沟藻的多甲藻叶绿素蛋白复合体

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

作者信息

Hofmann E, Wrench P M, Sharples F P, Hiller R G, Welte W, Diederichs K

机构信息

Fakultät für Biologie, Universität Konstanz, Germany.

出版信息

Science. 1996 Jun 21;272(5269):1788-91. doi: 10.1126/science.272.5269.1788.

DOI:10.1126/science.272.5269.1788
PMID:8650577
Abstract

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.

摘要

多甲藻素-叶绿素蛋白是一种水溶性捕光复合体,其主要色素为吸收蓝绿光的类胡萝卜素,存在于大多数光合甲藻中。其高分辨率(2.0埃)X射线结构揭示了一个非晶体三聚体,其中每个多肽包含α-螺旋氨基端和羧基端结构域的异常果冻卷折叠。这些结构域构成了一个具有伪二重对称性的支架,围绕着一个由两个脂质、八个多甲藻素和两个叶绿素a分子填充的疏水腔。从多甲藻素到叶绿素的高效激子能量转移的结构基础在于多甲藻素在范德华距离下围绕叶绿素的聚集。

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