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6S5L

Anabaena Apo-C-Terminal Domain Homolog Of The Orange Carotenoid Protein In Native Conditions

Summary for 6S5L
Entry DOI10.2210/pdb6s5l/pdb
DescriptorAll4940 protein (2 entities in total)
Functional Keywordsocp, orange carotenod protein, carotenoid transfer, ctdh, apoctdh, ctt, photosynthesis
Biological sourceNostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Total number of polymer chains12
Total formula weight181609.37
Authors
Harris, D.,Muzzopappa, F.,Kirilovsky, D.,Adir, N. (deposition date: 2019-07-01, release date: 2020-05-13, Last modification date: 2024-10-23)
Primary citationHarris, D.,Muzzopappa, F.,Glaser, F.,Wilson, A.,Kirilovsky, D.,Adir, N.
Structural dynamics in the C terminal domain homolog of orange carotenoid Protein reveals residues critical for carotenoid uptake.
Biochim Biophys Acta Bioenerg, 1861:148214-148214, 2020
Cited by
PubMed 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.
PubMed: 32360310
DOI: 10.1016/j.bbabio.2020.148214
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

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