Heptameric association of light-harvesting complex II trimers in partially solubilized photosystem II membranes.
We report a structural characterization by electron microscopy and image analysis of a supramolecular complex consisting of seven trimeric light-harvesting complex II proteins. The complex was readily observed in partially-solubilized Tris-washed photosystem II membranes from spinach but was also found to occur, with a low frequency, in oxygen-evolving photosystem II membranes. The structure reveals six peripheral trimers with the same rotational orientation and a central trimer with the opposite orientation. We conclude that the heptamer represents a naturally occurring aggregation state of part of the light-harvesting complex II trimers in the thylakoid membranes.
Dekker
J P
JP
Dept. of Physics and Astronomy, Institute of Molecular Biological Sciences, Vrije Universiteit, Amsterdam, The Netherlands.
van Roon
H
H
Boekem
E J
EJ
D003902:Detergents; D005960:Glucosides; D008566:Membranes / Q000648:ultrastructure; D008854:Microscopy, Electron; D045322:Photosynthetic Reaction Center Complex Proteins / Q000648:ultrastructure*; D045332:Photosystem II Protein Complex; D012995:Solubility
D003902:Detergents; D005960:Glucosides; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; C040358:dodecyl maltoside