PDBsum entry 1vcr

Photosynthesis

PDB id: 1vcr

Contents

Protein chain

101 a.a. *

Ligands

CLA ×7

CHL ×5

* Residue conservation analysis

PDB id:

1vcr

Name:

Photosynthesis

Title:

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

Structure:

Chlorophyll a-b binding protein ab80. Chain: a. Synonym: light-harvesting chlorophyll a/b protein, lhcii type i cab- ab80, lhcp

Source:

Pisum sativum. Pea. Organism_taxid: 3888. Tissue: thylakoid membrane

Resolution:

9.50Å R-factor: 0.379 R-free: 0.353

Authors:

T.Hino,E.Kanamori,J.-R.Shen,T.Kouyama

Key ref:

T.Hino et al. (2004). An icosahedral assembly of the light-harvesting chlorophyll a/b protein complex from pea chloroplast thylakoid membranes. Acta Crystallogr D Biol Crystallogr, 60, 803-809. PubMed id: 15103124 DOI: 10.1107/S0907444904003233

Date:

10-Mar-04 Release date: 30-Mar-04

Protein chain

P07371  (CB22_PEA) -  Chlorophyll a-b binding protein AB80, chloroplastic from Pisum sativum

Seq: 269 a.a.

Struc: 101 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1107/S0907444904003233

Acta Crystallogr D Biol Crystallogr 60:803-809 (2004)

PubMed id: 15103124

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

T.Hino, E.Kanamori, J.R.Shen, T.Kouyama.

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 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.

Selected figure(s)

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.

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] ).

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2004, 60, 803-809) copyright 2004.

Figures were selected by the author.