Abstract
The structural features enabling carotenoid translocation between molecular entities in nature is poorly understood. Here, we present the three-dimensional X-ray structure of an expanded oligomeric state of the C-terminal domain homolog (CTDH) of the orange carotenoid protein, a key water-soluble protein in cyanobacterial photosynthetic photo-protection, at 2.9 Å resolution. This protein binds a canthaxanthin carotenoid ligand and undergoes structural reorganization at the dimeric level, which facilitates cargo uptake and delivery. The structure displays heterogeneity revealing the dynamic nature of its C-terminal tail (CTT). Molecular dynamics (MD) simulations based on the CTDH structures identified specific residues that govern the dimeric transition mechanism. Mutagenesis based on the crystal structure and these MD simulations then confirmed that these specific residues within the CTT are critical for carotenoid uptake, encapsulation and delivery processes. We present a mechanism that can be applied to other systems that require cargo uptake.
Original language | English |
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Article number | 148214 |
Journal | Biochimica et Biophysica Acta - Bioenergetics |
Volume | 1861 |
Issue number | 8 |
DOIs | |
State | Published - 1 Aug 2020 |
Keywords
- Cyanobacteria
- Ligand transfer
- Molecular dynamics
- Mutagenesis
- Photoprotection
- X-ray crystallography
All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Cell Biology