ジャーナル: Nat Commun / 年: 2018 タイトル: OCP-FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria. 著者: Nikolai N Sluchanko / Yury B Slonimskiy / Evgeny A Shirshin / Marcus Moldenhauer / Thomas Friedrich / Eugene G Maksimov / 要旨: In cyanobacteria, high light photoactivates the orange carotenoid protein (OCP) that binds to antennae complexes, dissipating energy and preventing the destruction of the photosynthetic apparatus. At ...In cyanobacteria, high light photoactivates the orange carotenoid protein (OCP) that binds to antennae complexes, dissipating energy and preventing the destruction of the photosynthetic apparatus. At low light, OCP is efficiently deactivated by a poorly understood action of the dimeric fluorescence recovery protein (FRP). Here, we engineer FRP variants with defined oligomeric states and scrutinize their functional interaction with OCP. Complemented by disulfide trapping and chemical crosslinking, structural analysis in solution reveals the topology of metastable complexes of OCP and the FRP scaffold with different stoichiometries. Unable to tightly bind monomeric FRP, photoactivated OCP recruits dimeric FRP, which subsequently monomerizes giving 1:1 complexes. This could be facilitated by a transient OCP-2FRP-OCP complex formed via the two FRP head domains, significantly improving FRP efficiency at elevated OCP levels. By identifying key molecular interfaces, our findings may inspire the design of optically triggered systems transducing light signals into protein-protein interactions.
登録者
Nikolai Sluchanko (A.N. Bach Institute of Biochemistry, Moscow, Russia)
設備名称: PETRA III EMBL P12 / 地域: Hamburg / 国: Germany / 線源: X-ray synchrotron / 波長: 0.124 Å
検出器
名称: Pilatus 2M
スキャン
タイトル: Synechocystis fluorescence recovery protein FRPcc in the pre-oxidized state (CC mutant) 測定日: 2017年9月1日 / 保管温度: 20 °C / セル温度: 10 °C / 照射時間: 0.05 sec. / フレーム数: 20 / 単位: 1/nm /