4XB4

Structure of the N-terminal domain of OCP binding canthaxanthin

4XB4 の概要

• エントリーDOI: 10.2210/pdb4xb4/pdb
• 関連するPDBエントリー: 4XB5
• 分子名称: Orange carotenoid-binding protein, beta,beta-carotene-4,4'-dione (3 entities in total)
• 機能のキーワード: photoprotection, carotenoid binding protein
• 由来する生物種: Synechocystis sp.
• 細胞内の位置: Cellular thylakoid membrane ; Peripheral membrane protein ; Cytoplasmic side : P74102
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34339.66

構造登録者

Kerfeld, C.A.,Sutter, M.,Leverenz, R.L. (登録日: 2014-12-16, 公開日: 2015-07-15, 最終更新日: 2023-09-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.544 Å)