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

Structure determination of the seven-helix transmembrane receptor sensory rhodopsin II by solution NMR spectroscopy.
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DOI:
10.1038/nsmb.1807
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发表时间:
2010-06
影响因子:
16.8
通讯作者:
--
中科院分区:
生物学1区
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七螺旋膜蛋白是结构生物学的一个挑战。在这里,我们首次报道了洗涤剂溶解的七螺旋跨膜(7TM)蛋白的核磁共振结构测定,作为原理的证明。该结构的整体质量非常好(主干均方根偏差为0.48?),与先前确定的X射线结构非常吻合。此外,在更像天然的小磷脂双链中的测量表明,蛋白质结构与洗涤剂胶束中的相同,这表明使用温和洗涤剂时对环境的影响微乎其微。我们以我们的案例研究为平台,讨论对包括G蛋白偶联受体(GPCRs)家族成员在内的其他7TM蛋白进行类似溶液核磁共振研究的可行性。
Seven-helical membrane proteins represent a challenge for structural biology. Here, we report the first NMR structure determination of a detergent-solubilized seven-helical 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 extremely good (backbone root mean squared deviation of 0.48 Å) 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 (GPCRs).
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