Brominated lipids identify lipid binding sites on the surface of the reaction center from Rhodobacter sphaeroides.
This study describes the use of brominated phospholipids to distinguish between lipid and detergent binding sites on the surface of a typical alpha-helical membrane protein. Reaction centers isolated from Rhodobacter sphaeroides were cocrystallized with added brominated phospholipids. X-ray structural analysis of these crystals has revealed the presence of two lipid binding sites from the characteristic strong X-ray scattering from the bromine atoms. These results demonstrate the usefulness of this approach to mapping lipid binding sites at the surface of membrane proteins.
Roszak
Aleksander W
AW
Department of Chemistry, WestCHEM.
Gardiner
Alastair T
AT
Isaacs
Neil W
NW
Cogdell
Richard J
RJ
D001665:Binding Sites; D001966:Bromine; D003460:Crystallization; D018360:Crystallography, X-Ray; D020404:Glycerophospholipids / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D012242:Rhodobacter sphaeroides / Q000737:chemistry* / Q000378:metabolism
D020404:Glycerophospholipids; D008565:Membrane Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D001966:Bromine