Solution NMR mapping of water-accessible residues in the transmembrane beta-barrel of OmpX.
Eur Biophys J
; 39(4): 623-30, 2010 Mar.
Article
in En
| MEDLINE
| ID: mdl-19639312
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 beta-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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacterial Outer Membrane Proteins
/
Water
/
Cell Membrane
/
Nuclear Magnetic Resonance, Biomolecular
/
Escherichia coli Proteins
/
Hydrolases
Language:
En
Journal:
Eur Biophys J
Journal subject:
BIOFISICA
Year:
2010
Type:
Article
Affiliation country:
France