4XB4

Structure of the N-terminal domain of OCP binding canthaxanthin

Summary for 4XB4

• Entry DOI: 10.2210/pdb4xb4/pdb
• Related: 4XB5
• Descriptor: Orange carotenoid-binding protein, beta,beta-carotene-4,4'-dione (3 entities in total)
• Functional Keywords: photoprotection, carotenoid binding protein
• Biological source: Synechocystis sp.
• Cellular location: Cellular thylakoid membrane ; Peripheral membrane protein ; Cytoplasmic side : P74102
• Total number of polymer chains: 2
• Total formula weight: 34339.66

Authors

Kerfeld, C.A.,Sutter, M.,Leverenz, R.L. (deposition date: 2014-12-16, release date: 2015-07-15, Last modification date: 2023-09-27)

Primary citation

Leverenz, R.L.,Sutter, M.,Wilson, A.,Gupta, S.,Thurotte, A.,Bourcier de Carbon, C.,Petzold, C.J.,Ralston, C.,Perreau, F.,Kirilovsky, D.,Kerfeld, C.A.
PHOTOSYNTHESIS. A 12 angstrom carotenoid translocation in a photoswitch associated with cyanobacterial photoprotection.
Science, 348:1463-1466, 2015

PubMed Abstract: Pigment-protein and pigment-pigment interactions are of fundamental importance to the light-harvesting and photoprotective functions essential to oxygenic photosynthesis. The orange carotenoid protein (OCP) functions as both a sensor of light and effector of photoprotective energy dissipation in cyanobacteria. We report the atomic-resolution structure of an active form of the OCP consisting of the N-terminal domain and a single noncovalently bound carotenoid pigment. The crystal structure, combined with additional solution-state structural data, reveals that OCP photoactivation is accompanied by a 12 angstrom translocation of the pigment within the protein and a reconfiguration of carotenoid-protein interactions. Our results identify the origin of the photochromic changes in the OCP triggered by light and reveal the structural determinants required for interaction with the light-harvesting antenna during photoprotection.

PubMed: 26113721
DOI: 10.1126/science.aaa7234

Experimental method

X-RAY DIFFRACTION (1.544 Å)