TITLE

Solution NMR mapping of water-accessible residues in the transmembrane β-barrel of OmpX

AUTHOR(S)
Catoire, Laurent J.; Zoonens, Manuela; van Heijenoort, Carine; Giusti, Fabrice; Guittet, Éric; Popot, Jean-Luc
PUB. DATE
March 2010
SOURCE
European Biophysics Journal;Mar2010, Vol. 39 Issue 4, p623
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
The atomic structure of OmpX, the smallest member of the bacterial outer membrane protein family, has been previously established by X-ray crystallography and NMR spectroscopy. In apparent conflict with electrophysiological studies, the lumen of its transmembrane β-barrel appears too tightly packed with amino acid side chains to let any solute flow through. In the present study, high-resolution solution NMR spectra were obtained of OmpX kept water-soluble by either amphipol A8-35 or the detergent dihexanoylphosphatidylcholine. Hydrogen/deuterium exchange measurements performed after prolonged equilibration show that, whatever the surfactant used, some of the amide protons of the membrane-spanning region exchange much more readily than others, which likely reflects the dynamics of the barrel.
ACCESSION #
48624270

 

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