Solution NMR Structure of Proteorhodopsin

被引:142
作者
Reckel, Sina [1 ,2 ]
Gottstein, Daniel [1 ,2 ]
Stehle, Jochen [2 ,3 ]
Loehr, Frank [1 ,2 ]
Verhoefen, Mirka-Kristin [4 ]
Takeda, Mitsuhiro [5 ]
Silvers, Robert [2 ,3 ]
Kainosho, Masatsune [5 ,7 ]
Glaubitz, Clemens [1 ,2 ]
Wachtveitl, Josef [4 ]
Bernhard, Frank [1 ,2 ]
Schwalbe, Harald [2 ,3 ]
Guentert, Peter [1 ,2 ,6 ,7 ]
Doetsch, Volker [1 ,2 ]
机构
[1] Goethe Univ Frankfurt, Inst Biophys Chem, D-60438 Frankfurt, Germany
[2] Goethe Univ Frankfurt, Ctr Biomol Magnet Resonance, D-60438 Frankfurt, Germany
[3] Goethe Univ Frankfurt, Inst Organ Chem & Chem Biol, D-60438 Frankfurt, Germany
[4] Goethe Univ Frankfurt, Inst Phys & Theoret Chem, D-60438 Frankfurt, Germany
[5] Nagoya Univ, Struct Biol Res Ctr, Chikusa Ku, Nagoya, Aichi 4648601, Japan
[6] Goethe Univ Frankfurt, Frankfurt Inst Adv Studies, D-60438 Frankfurt, Germany
[7] Tokyo Metropolitan Univ, Ctr Prior Areas, Hachioji, Tokyo 1920397, Japan
基金
日本学术振兴会;
关键词
membrane proteins; NMR spectroscopy; proteorhodopsin; structural biology; NUCLEAR-MAGNETIC-RESONANCE; RETINAL SCHIFF-BASE; DRIVEN PROTON PUMP; SOLID-STATE NMR; PROTEINS; CHROMOPHORE; EXPRESSION; RHODOPSIN; DYNAMICS; FRAGMENT;
D O I
10.1002/anie.201105648
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
A solved puzzle: The structure of the seven-transmembrane-helix proton pump proteorhodopsin obtained by solution NMR spectroscopy is based on NOE data combined with distance restraints derived from paramagnetic relaxation enhancement (see picture). Restraints from residual dipolar couplings improved the structural accuracy. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
引用
收藏
页码:11942 / 11946
页数:5
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