AG Proteinkristallographie, Department of Biophysics, Faculty of Biology and Biotechnology, Gebäude ND 04/316, Ruhr-University Bochum, 44780 Bochum, Germany.
Eur J Cell Biol. 2010 Dec;89(12):990-7. doi: 10.1016/j.ejcb.2010.08.004. Epub 2010 Sep 16.
Peridinin-chlorophyll a-proteins are a class of light-harvesting proteins only found in photosynthetic dinoflagellates. Due to their exceptional stability they are an excellent model system to study carotenoid to chlorophyll energy transfer. We were able to solve structures of these complexes at near atomic resolution, allowing the detailed discussion of pigment-pigment and pigment-protein interactions. Using a refolding system, we also determined structures of complexes with mutated apoproteins and modified pigment compositions. Here we summarize the current understanding of PCP structures, with an emphasis on how the basic dimeric structure may be modified in the oligomeric state of these complexes.
原卟啉啉-叶绿素 a 蛋白是一类仅存在于光合甲藻中的光捕获蛋白。由于其特殊的稳定性，它们是研究类胡萝卜素向叶绿素能量转移的极好模型系统。我们能够以近原子分辨率解决这些复合物的结构，从而可以详细讨论色素-色素和色素-蛋白相互作用。使用复性系统，我们还确定了具有突变 apoproteins 和修饰的色素组成的复合物的结构。在这里，我们总结了目前对 PCP 结构的理解，重点介绍了在这些复合物的寡聚状态下，基本二聚体结构如何被修饰。
