4XB5

Structure of orange carotenoid protein binding canthaxanthin

Summary for 4XB5

• Entry DOI: 10.2210/pdb4xb5/pdb
• Related: 4XB4
• Descriptor: Orange carotenoid-binding protein, beta,beta-carotene-4,4'-dione, GLYCEROL, ... (4 entities in total)
• Functional Keywords: carotenoid-binding, photoprotection, carotenoid binding protein
• Biological source: Synechocystis sp. (strain PCC 6803 / Kazusa)
• Cellular location: Cellular thylakoid membrane : P74102
• Total number of polymer chains: 1
• Total formula weight: 36401.62

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 (1.9 Å)