1VCR
An icosahedral assembly of light-harvesting chlorophyll a/b protein complex from pea thylakoid membranes
Summary for 1VCR
| Entry DOI | 10.2210/pdb1vcr/pdb |
| Descriptor | Chlorophyll a-b binding protein AB80, CHLOROPHYLL A, CHLOROPHYLL B (3 entities in total) |
| Functional Keywords | lhc-ii, icosahedron, chlorophyll, antenna, photosystem, photosynthesis |
| Biological source | Pisum sativum (pea) |
| Total number of polymer chains | 1 |
| Total formula weight | 35727.90 |
| Authors | Hino, T.,Kanamori, E.,Shen, J.-R.,Kouyama, T. (deposition date: 2004-03-10, release date: 2004-03-30, Last modification date: 2024-04-03) |
| Primary citation | Hino, T.,Kanamori, E.,Shen, J.R.,Kouyama, T. An icosahedral assembly of the light-harvesting chlorophyll a/b protein complex from pea chloroplast thylakoid membranes. Acta Crystallogr.,Sect.D, 60:803-809, 2004 Cited by PubMed 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. PubMed: 15103124DOI: 10.1107/S0907444904003233 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (9.5 Å) |
Structure validation
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