An icosahedral assembly of the light-harvesting chlorophyll a/b protein complex from pea chloroplast thylakoid membranes.
When the light-harvesting chlorophyll a/b protein complex (LHC-II) from pea thylakoid membranes is co-crystallized with native lipids, an octahedral crystal that exhibits no birefringence is obtained. Cryogenic electron micrographs of a crystal edge showed the crystal to be made up of hollow spherical assemblies with a diameter of 250 A. X-ray diffraction data at 9.5 A resolution revealed the spherical shell of LHC-II to have icosahedral symmetry. A T = 1 icosahedral model of LHC-II, in which the stromal surface of the protein faces outward, was constructed using the previously reported structure of the LHC-II trimer [Kühlbrandt et al. (1994), Nature (London), 367, 614-621]. The present result shows the first example of a well ordered three-dimensional crystal of icosahedral proteoliposomes.
Hino
Tomoya
T
Department of Physics, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan.
Kanamori
Eiji
E
Shen
Jian-Ren
JR
Kouyama
Tsutomu
T
D003460:Crystallization; D018360:Crystallography, X-Ray; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry*; D008854:Microscopy, Electron; D008958:Models, Molecular; D018532:Pisum sativum / Q000737:chemistry*; D011487:Protein Conformation; D020524:Thylakoids / Q000737:chemistry*
D045342:Light-Harvesting Protein Complexes