ArticleScientific reports2020
Structural analysis of a new carotenoid-binding protein: the C-terminal domain homolog of the OCP.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 28 citations in OpenAlex.
- Protein/linker dynamics facilitates the structural adaptation of the orange carotenoid protein in cyanobacterial photoprotection: a neutron scattering study.Photosynthesis research · 2026Article
- N-Terminal domain homologs of the orange carotenoid protein increase quenching of cyanobacterial phycobilisomes.Plant physiology · 2025Article
- Enabling simultaneous photoluminescence spectroscopy and X-ray footprinting mass spectrometry to study protein conformation and interactions.Analytical methods : advancing methods and applications · 2025Article
- Multiplex Trifluoromethyl and Hydroxyl Radical Chemistry Enables High-Resolution Protein Footprinting.Analytical chemistry · 2025Article
- Light sensitive orange carotenoid proteins (OCPs) in cyanobacterial photoprotection: evolutionary insights, structural-functional dynamics and biotechnological prospects.Archives of microbiology · 2025Review
- Recent Progress in Solution Structure Studies of Photosynthetic Proteins Using Small-Angle Scattering Methods.Molecules (Basel, Switzerland) · 2023Review
- Structural basis for the ligand promiscuity of the neofunctionalized, carotenoid-binding fasciclin domain protein AstaP.Communications biology · 2023Article
- Integrated Structural Studies for Elucidating Carotenoid-Protein Interactions.Advances in experimental medicine and biology · 2022Article
- Heterologous expression of cyanobacterial Orange Carotenoid Protein (OCP2) as a soluble carrier of ketocarotenoids inAlgal research · 2021Article
- Environmental Tuning of Homologs of the Orange Carotenoid Protein-Encoding Gene in the CyanobacteriumFrontiers in microbiology · 2021Article
- Comparison of angiopoietin-like protein 3 and 4 reveals structural and mechanistic similarities.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
The Orange Carotenoid Protein (OCP) is a water-soluble protein that governs photoprotection in many cyanobacteria. The 35 kDa OCP is structurally and functionally modular, consisting of an N-terminal effector domain (NTD) and a C-terminal regulatory domain (CTD); a carotenoid spans the two domains. The CTD is a member of the ubiquitous Nuclear Transport Factor-2 (NTF2) superfamily (pfam02136). With the increasing availability of cyanobacterial genomes, bioinformatic analysis has revealed the existence of a new family of proteins, homologs to the CTD, the C-terminal domain-like carotenoid proteins (CCPs). Here we purify holo-CCP2 directly from cyanobacteria and establish that it natively binds canthaxanthin (CAN). We use small-angle X-ray scattering (SAXS) to characterize the structure of this carotenoprotein in two distinct oligomeric states. A single carotenoid molecule spans the two CCPs in the dimer. Our analysis with X-ray footprinting-mass spectrometry (XFMS) identifies critical residues for carotenoid binding that likely contribute to the extreme red shift (ca. 80 nm) of the absorption maximum of the carotenoid bound by the CCP2 dimer and a further 10 nm shift in the tetramer form. These data provide the first structural description of carotenoid binding by a protein consisting of only an NTF2 domain.
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