Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR.
Recent progress from our laboratories to determine structures of small membrane proteins (up to 20 kDa) in detergent micelles by solution nuclear magnetic resonance (NMR) is reviewed. NMR opens a new window to also study, for the first time, the dynamics of membrane proteins. We report on recent attempts to correlate dynamic measurements on OmpA with the ion channel function of this protein. We also summarize how NMR and spin-label electron paramagnetic resonance spectroscopy and selective mutagenesis can be combined to provide a structural basis towards understanding the mechanism of influenza hemagglutinin-mediated membrane fusion.
Tamm
Lukas K
LK
Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908-0736, USA. lkt2e@virginia.edu
Abildgaard
Frits
F
Arora
Ashish
A
Blad
Heike
H
Bushweller
John H
JH
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D003902:Detergents; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry* / Q000378:metabolism; D008823:Micelles; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D012996:Solutions; D013816:Thermodynamics; D014760:Viral Fusion Proteins / Q000737:chemistry / Q000378:metabolism
D001425:Bacterial Outer Membrane Proteins; D003902:Detergents; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D008823:Micelles; D012996:Solutions; D014760:Viral Fusion Proteins; C078167:OMPA outer membrane proteins