An icosahedral assembly of the light-harvesting chlorophyll a/b protein complex from pea chloroplast thylakoid membranes

Authors: Hino, Tomoya; Kanamori, Eiji; Shen, Jian-Ren; Kouyama, Tsutomu

Source: Acta Crystallographica Section D, Volume 60, Number 5, May 2004 , pp. 803-809(7)

Publisher: Blackwell Publishing

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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 Å. X-ray diffraction data at 9.5 Å 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.

Keywords: light-harvesting complex; photosystem II antenna; bacteriorhodopsin; membrane protein; icosahedral assembly

Document Type: Research article

DOI: 10.1107/S0907444904003233

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