1vcr

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(New page: 200px<br /><applet load="1vcr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vcr, resolution 9.5&Aring;" /> '''An icosahedral assemb...)
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Revision as of 02:28, 21 November 2007

Image:1vcr.gif

1vcr, resolution 9.5Å

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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

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