7QD1
Structure of the orange carotenoid protein from Planktothrix agardhii binding echinenone in the P21 space group
Summary for 7QD1
| Entry DOI | 10.2210/pdb7qd1/pdb |
| Descriptor | Orange carotenoid-binding protein, beta,beta-caroten-4-one (3 entities in total) |
| Functional Keywords | carotenoid-binding, photoprotection, carotenoid binding protein, photosynthesis |
| Biological source | Planktothrix agardhii (Oscillatoria agardhii) |
| Total number of polymer chains | 2 |
| Total formula weight | 71806.58 |
| Authors | Andreeva, E.A.,Hartmann, E.,Schlichting, I.,Colletier, J.-P. (deposition date: 2021-11-26, release date: 2022-07-06, Last modification date: 2024-11-13) |
| Primary citation | Wilson, A.,Andreeva, E.A.,Nizinski, S.J.,Talbot, L.,Hartmann, E.,Schlichting, I.,Burdzinski, G.,Sliwa, M.,Kirilovsky, D.,Colletier, J.P. Structure-function-dynamics relationships in the peculiar Planktothrix PCC7805 OCP1: Impact of his-tagging and carotenoid type. Biochim Biophys Acta Bioenerg, 1863:148584-148584, 2022 Cited by PubMed Abstract: The orange carotenoid protein (OCP) is a photoactive protein involved in cyanobacterial photoprotection. Here, we report on the functional, spectral and structural characteristics of the peculiar Planktothrix PCC7805 OCP (Plankto-OCP). We show that this OCP variant is characterized by higher photoactivation and recovery rates, and a stronger energy-quenching activity, compared to other OCP studied thus far. We characterize the effect of the functionalizing carotenoid and of his-tagging on these reactions, and identify the time scales on which these modifications affect photoactivation. The presence of a his-tag at the C-terminus has a large influence on photoactivation, thermal recovery and PBS-fluorescence quenching, and likewise for the nature of the carotenoid that additionally affects the yield and characteristics of excited states and the ns-s dynamics of photoactivated OCP. By solving the structures of Plankto-OCP in the ECN- and CAN-functionalized states, each in two closely-related crystal forms, we further unveil the molecular breathing motions that animate Plankto-OCP at the monomer and dimer levels. We finally discuss the structural changes that could explain the peculiar properties of Plankto-OCP. PubMed: 35752265DOI: 10.1016/j.bbabio.2022.148584 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.71 Å) |
Structure validation
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