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PDBsum entry 1vcr
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Photosynthesis
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PDB id
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1vcr
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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An icosahedral assembly of the light-Harvesting chlorophyll a/b protein complex from pea chloroplast thylakoid membranes.
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Authors
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T.Hino,
E.Kanamori,
J.R.Shen,
T.Kouyama.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2004,
60,
803-809.
[DOI no: ]
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PubMed id
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Abstract
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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
[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.
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Figure 1.
Figure 1 Electron micrographs of the vesicular assemblies of
LHC-II. (a) Cryogenic electron micrograph of a peripheral edge
of the octahedral crystal of LHC-II. Small crystals of LHC-II
were grown in a solution containing 50 mM KCl, 10 mM HEPES pH
7.0 and 0.6%(w/v) nonyl glucoside and rapidly cooled with liquid
propane. (b) Cryogenic electron micrograph of a
pre-crystallizing solution of LHC-II containing 20 mM KCl, 10
mM HEPES pH 7.0 and 0.6%(w/v) nonyl glucoside. The bar
represents 100 nm.
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Figure 5.
Figure 5 Structure of the icosahedral assembly of LHC-II. (a)
View of the whole assembly along a twofold symmetry axis,
overlaid on a T = 1 icosahedral lattice (white line).
Polypeptides are drawn in a ribbon representation (gold) and
chlorophylls are drawn in CPK representation (green). (b)
Enlarged view showing the relative positions of neighbouring
trimers. Each subunit of the protein is composed of three
transmembrane helices (A, B and C) and a short helix (D) located
near the lumenal surface of the membrane and 12 chlorophyll
molecules (shown as a wire model). The shaded arc represents a
hypothetical hydrophobic region of the lipid-detergent bilayer.
(a) was drawn with VMD (Humphrey et al., 1996[Humphrey, W.,
Dalke, A. & Schulten, K. (1996). J. Mol. Graph. 14, 33-38.]) and
POV-Ray ([148]http://www.povray.org ) and (b) with MOLSCRIPT
(Kraulis, 1991[149] [Kraulis, P. J. (1991). J. Appl. Cryst. 24,
946-950.]-[150][bluearr.gif] ) and RASTER3D (Merritt & Murphy,
1994[151] [Merritt, E. A. & Murphy, M. E. P. (1994). Acta Cryst.
D50, 869-873.]-[152][bluearr.gif] ).
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2004,
60,
803-809)
copyright 2004.
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