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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[[Image:1vcr.gif|left|200px]]<br /><applet load="1vcr" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1vcr, resolution 9.5&Aring;" />
caption="1vcr, resolution 9.5&Aring;" />
'''An icosahedral assembly of light-harvesting chlorophyll a/b protein complex from pea thylakoid membranes'''<br />
'''An icosahedral assembly of light-harvesting chlorophyll a/b protein complex from pea thylakoid membranes'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1VCR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with CLA and CHL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VCR OCA].
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1VCR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with <scene name='pdbligand=CLA:'>CLA</scene> and <scene name='pdbligand=CHL:'>CHL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCR OCA].
==Reference==
==Reference==
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[[Category: Kanamori, E.]]
[[Category: Kanamori, E.]]
[[Category: Kouyama, T.]]
[[Category: Kouyama, T.]]
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[[Category: Shen, J.R.]]
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[[Category: Shen, J R.]]
[[Category: CHL]]
[[Category: CHL]]
[[Category: CLA]]
[[Category: CLA]]
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[[Category: photosystem]]
[[Category: photosystem]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:35:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:52 2008''

Revision as of 13:33, 21 February 2008


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 and 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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