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

Abstract：

: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 A) 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.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Gautier A,Mott HR,Bostock MJ,Kirkpatrick JP,Nietlispach D

doi

10.1038/nsmb.1807

subject

Has Abstract

pub_date

2010-06-01 00:00:00

pages

768-74

issue

6

eissn

1545-9993

issn

1545-9985

pii

nsmb.1807

journal_volume

17

pub_type

杂志文章

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