SARS coronavirus E protein in phospholipid bilayers: an x-ray study.
We investigated the structure of the hydrophobic domain of the severe acute respiratory syndrome E protein in model lipid membranes by x-ray reflectivity and x-ray scattering. In particular, we used x-ray reflectivity to study the location of an iodine-labeled residue within the lipid bilayer. The label imposes spatial constraints on the protein topology. Experimental data taken as a function of protein/lipid ratio P/L and different swelling states support the hairpin conformation of severe acute respiratory syndrome E protein reported previously. Changes in the bilayer thickness and acyl-chain ordering are presented as a function of P/L, and discussed in view of different structural models.
Khattari
Z
Z
Institute for X-ray Physics, University of Göttingen, Göttingen, Germany.
Brotons
G
G
Akkawi
M
M
Arbely
E
E
Arkin
I T
IT
Salditt
T
T
D004134:Dimyristoylphosphatidylcholine / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry*; D008560:Membrane Fluidity; D008565:Membrane Proteins / Q000737:chemistry / Q000648:ultrastructure; D044367:Phase Transition; D010743:Phospholipids / Q000737:chemistry*; D011487:Protein Conformation; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D000086082:Viroporin Proteins; D014961:X-Ray Diffraction
C501689:E protein, SARS coronavirus; D008051:Lipid Bilayers; D008565:Membrane Proteins; D010743:Phospholipids; D014759:Viral Envelope Proteins; D000086082:Viroporin Proteins; D004134:Dimyristoylphosphatidylcholine