Higher order structure and function of retinal proteins

2014 Fiscal Year Final Research Report

• Project/Area Number: 24370066
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Partial Multi-year Fund
• Section: 一般
• Research Field: Biophysics
• Research Institution: Nagoya University
• Principal Investigator: KOUYAMA tsutomu 名古屋大学, 理学(系)研究科(研究院), 教授 (30170210)
• Co-Investigator(Kenkyū-buntansha): MURAKAMI Midori 名古屋大学, 理学研究科, 助教 (20324387) ; IHARA Kunio 名古屋大学, 遺伝子実験施設, 准教授 (90223297) ; IWASA Tatsuo 室蘭工業大学, 工学部, 教授 (00133926)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: レチナールタンパク質 / プロトン輸送性ロドプシン / 陰イオン輸送性ロドプシン / 無脊椎動物系ロドプシン / X線結晶構造解析 / ハロロドプシン / アーキロドプシン / 反応中間体

Outline of Final Research Achievements

① Archaerhodopsin-2　was crystallized and its structure was　determined at 1.8 Åresolution. ② Cruxrhodopsin-3 was crystallized and its structure was determined at 2.1 Å resolution.　③ Deltarhodopsin-3 was crystallized and its trimeric structure was determined at 2.7 Å resolution. ④ The light-driven chloride ion pump halorhodopsin (pHR) from Natronomonas pharonis was crystallized, and the major photoreaction states (L1, L2, N, N’and O states) of pHR-bromide ion complex were determined at 2.2 -2.7 Å resolutions. ⑤ The crystal structure of an M intermediate of pHR-azide complex was determined at 2.3 Å resolution. ⑥ Various　mutants of phoborhodopsin from Halobacterium　salinarum were prepared and their photoreaction kinetics were investigated. ⑦ The crystal structure of the Lumi state of squid rhodopsin was determined at 2.7 Å resolution. ⑧ Octopus　rhodopsin was crystallized by the membrane fusion method.

Free Research Field

生物物理