1. Orange carotenoid proteins: structural understanding of evolution and function
- Author
-
Kerfeld, Cheryl A and Sutter, Markus
- Subjects
Biochemistry and Cell Biology ,Biological Sciences ,Genetics ,Generic health relevance ,Bacterial Proteins ,Cyanobacteria ,Evolution ,Molecular ,Carotenoids ,carotenoids ,cyanobacteria ,photoprotection ,photosynthesis ,protein dynamics ,protein evolution ,Chemical Sciences ,Medical and Health Sciences ,Developmental Biology ,Biochemistry and cell biology ,Medical biochemistry and metabolomics ,Medicinal and biomolecular chemistry - Abstract
Cyanobacteria uniquely contain a primitive water-soluble carotenoprotein, the orange carotenoid protein (OCP). Nearly all extant cyanobacterial genomes contain genes for the OCP or its homologs, implying an evolutionary constraint for cyanobacteria to conserve its function. Genes encoding the OCP and its two constituent structural domains, the N-terminal domain, helical carotenoid proteins (HCPs), and its C-terminal domain, are found in the most basal lineages of extant cyanobacteria. These three carotenoproteins exemplify the importance of the protein for carotenoid properties, including protein dynamics, in response to environmental changes in facilitating a photoresponse and energy quenching. Here, we review new structural insights for these carotenoproteins and situate the role of the protein in what is currently understood about their functions.
- Published
- 2024