Download MendeleyAn icosahedral assembly of the light-harvesting chlorophyll a/b protein complex from pea chloroplast thylakoid membranes.
Hino, T., Kanamori, E., Shen, J.R., Kouyama, T.(2004) Acta Crystallogr D Biol Crystallogr 60: 803-809
- PubMed: 15103124
- DOI: https://doi.org/10.1107/S0907444904003233
- Primary Citation of Related Structures:
1VCR - PubMed Abstract:
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 [K¨¹hlbrandt 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.
Organizational Affiliation:
Department of Physics, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan.
