Three-dimensional structure of plant light-harvesting complex determined by electron crystallography.
The structure of the light-harvesting chlorophyll a/b-protein complex, a membrane protein serving as the major antenna of solar energy in plant photosynthesis, has been determined at 6 A resolution by electron crystallography. Within the complex, three membrane-spanning alpha helices and 15 chlorophyll molecules are resolved. There is an intramolecular diad relating two of the alpha helices and some of the chlorophylls. The spacing of the chlorophylls suggests energy transfer by delocalized exciton coupling and Förster mechanisms.
Kühlbrandt
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European Molecular Biology Laboratory, Heidelberg, Germany.
Wang
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DN
D002734:Chlorophyll / Q000737:chemistry; D000077194:Chlorophyll A; D002736:Chloroplasts / Q000737:chemistry; D003461:Crystallography; D045342:Light-Harvesting Protein Complexes; D008051:Lipid Bilayers / Q000737:chemistry; D008958:Models, Molecular; D015394:Molecular Structure; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D011487:Protein Conformation
D045342:Light-Harvesting Protein Complexes; D008051:Lipid Bilayers; D045322:Photosynthetic Reaction Center Complex Proteins; D002734:Chlorophyll; C037184:chlorophyll b; D000077194:Chlorophyll A