6FEJ

Anabaena Apo-C-Terminal Domain Homolog Protein

Summary for 6FEJ

• Entry DOI: 10.2210/pdb6fej/pdb
• Descriptor: All4940 protein, UREA (3 entities in total)
• Functional Keywords: carotene cyanobacteria photoprotection urea, photosynthesis
• Biological source: Nostoc sp. PCC 7120
• Total number of polymer chains: 2
• Total formula weight: 26766.07

Authors

Harris, D.,Wilson, A.,Muzzopappa, F.,Kirilovsky, D.,Adir, N. (deposition date: 2018-01-02, release date: 2018-07-18, Last modification date: 2024-10-23)

Primary citation

Harris, D.,Wilson, A.,Muzzopappa, F.,Sluchanko, N.N.,Friedrich, T.,Maksimov, E.G.,Kirilovsky, D.,Adir, N.
Structural rearrangements in the C-terminal domain homolog of Orange Carotenoid Protein are crucial for carotenoid transfer.
Commun Biol, 1:125-125, 2018

PubMed Abstract: A recently reported family of soluble cyanobacterial carotenoproteins, homologs of the C-terminal domain (CTDH) of the photoprotective Orange Carotenoid Protein, is suggested to mediate carotenoid transfer from the thylakoid membrane to the Helical Carotenoid Proteins, which are paralogs of the N-terminal domain of the OCP. Here we present the three-dimensional structure of a carotenoid-free CTDH variant from () PCC 7120. This CTDH contains a cysteine residue at position 103. Two dimer-forming interfaces were identified, one stabilized by a disulfide bond between monomers and the second between each monomer's β-sheets, both compatible with small-angle X-ray scattering data and likely representing intermediates of carotenoid transfer processes. The crystal structure revealed a major positional change of the C-terminal tail. Further mutational analysis revealed the importance of the C-terminal tail in both carotenoid uptake and delivery. These results have allowed us to suggest a detailed model for carotenoid transfer via these soluble proteins.

PubMed: 30272005
DOI: 10.1038/s42003-018-0132-5

Experimental method

X-RAY DIFFRACTION (2.75 Å)