Structural Diversity in Eukaryotic Photosynthetic Light Harvesting.
Annu Rev Plant Biol
; 75(1): 119-152, 2024 Jul.
Article
em En
| MEDLINE
| ID: mdl-38360524
ABSTRACT
Photosynthesis has been using energy from sunlight to assimilate atmospheric CO2 for at least 3.5 billion years. Through evolution and natural selection, photosynthetic organisms have flourished in almost all aquatic and terrestrial environments. This is partly due to the diversity of light-harvesting complex (LHC) proteins, which facilitate photosystem assembly, efficient excitation energy transfer, and photoprotection. Structural advances have provided angstrom-level structures of many of these proteins and have expanded our understanding of the pigments, lipids, and residues that drive LHC function. In this review, we compare and contrast recently observed cryo-electron microscopy structures across photosynthetic eukaryotes to identify structural motifs that underlie various light-harvesting strategies. We discuss subtle monomer changes that result in macroscale reorganization of LHC oligomers. Additionally, we find recurring patterns across diverse LHCs that may serve as evolutionary stepping stones for functional diversification. Advancing our understanding of LHC protein-environment interactions will improve our capacity to engineer more productive crops.
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Base de dados:
MEDLINE
Assunto principal:
Fotossíntese
/
Complexos de Proteínas Captadores de Luz
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article