1vcr
From Proteopedia
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An icosahedral assembly of light-harvesting chlorophyll a/b protein complex from pea thylakoid membranes
Overview
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 [Kuhlbrandt 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.
About this Structure
1VCR is a Single protein structure of sequence from Pisum sativum with CLA and CHL as ligands. Full crystallographic information is available from OCA.
Reference
An icosahedral assembly of the light-harvesting chlorophyll a/b protein complex from pea chloroplast thylakoid membranes., Hino T, Kanamori E, Shen JR, Kouyama T, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):803-9. Epub 2004, Apr 21. PMID:15103124
Page seeded by OCA on Wed Nov 21 04:35:33 2007
Categories: Pisum sativum | Single protein | Hino, T. | Kanamori, E. | Kouyama, T. | Shen, J.R. | CHL | CLA | Antenna | Chlorophyll | Icosahedron | Lhc-ii | Photosystem
