Atomic model of plant light-harvesting complex by electron crystallography.
The structure of the light-harvesting chlorophyll a/b-protein complex, an integral membrane protein, has been determined at 3.4 A resolution by electron crystallography of two-dimensional crystals. Two of the three membrane-spanning alpha-helices are held together by ion pairs formed by charged residues that also serve as chlorophyll ligands. In the centre of the complex, chlorophyll a is in close contact with chlorophyll b for rapid energy transfer, and with two carotenoids that prevent the formation of toxic singlet oxygen.
Kühlbrandt
W
W
European Molecular Biology Laboratory, Heidelberg, Germany.
Wang
D N
DN
Fujiyoshi
Y
Y
D000595:Amino Acid Sequence; D002734:Chlorophyll / Q000737:chemistry; D017124:Conserved Sequence; D003461:Crystallography / Q000379:methods; D045342:Light-Harvesting Protein Complexes; D014975:Lutein / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry; D008854:Microscopy, Electron; D008958:Models, Molecular; D008969:Molecular Sequence Data; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D017433:Protein Structure, Secondary
D045342:Light-Harvesting Protein Complexes; D008565:Membrane Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D002734:Chlorophyll; D014975:Lutein