Abstract
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.
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