Structure determination of the seven-helix transmembrane receptor sensory rhodopsin II by solution NMR spectroscopy

被引:160
作者
Gautier, Antoine [1 ]
Mott, Helen R. [1 ]
Bostock, Mark J. [1 ]
Kirkpatrick, John P. [1 ]
Nietlispach, Daniel [1 ]
机构
[1] Univ Cambridge, Dept Biochem, Cambridge CB2 1QW, England
基金
英国生物技术与生命科学研究理事会; 英国惠康基金;
关键词
PROTEIN-COUPLED RECEPTORS; RESIDUAL DIPOLAR COUPLINGS; NUCLEAR-MAGNETIC-RESONANCE; INTEGRAL MEMBRANE ENZYME; LARGE-SCALE PRODUCTION; X-RAY-STRUCTURE; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; FUNCTIONAL EXPRESSION; CHEMICAL-SHIFT;
D O I
10.1038/nsmb.1807
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Seven-helix membrane proteins represent a challenge for structural biology. Here we report the first NMR structure determination of a detergent-solubilized seven-helix transmembrane (7TM) protein, the phototaxis receptor sensory rhodopsin II (pSRII) from Natronomonas pharaonis, as a proof of principle. The overall quality of the structure ensemble is good (backbone r.m.s. deviation of 0.48 angstrom) and agrees well with previously determined X-ray structures. Furthermore, measurements in more native-like small phospholipid bicelles indicate that the protein structure is the same as in detergent micelles, suggesting that environment-specific effects are minimal when using mild detergents. We use our case study as a platform to discuss the feasibility of similar solution NMR studies for other 7TM proteins, including members of the family of G protein-coupled receptors.
引用
收藏
页码:768 / U147
页数:8
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