1RWT

Crystal Structure of Spinach Major Light-harvesting complex at 2.72 Angstrom Resolution

Summary for 1RWT

• Entry DOI: 10.2210/pdb1rwt/pdb
• Descriptor: Chlorophyll A-B binding protein, chloroplast, CHLOROPHYLL A, nonyl beta-D-glucopyranoside, ... (11 entities in total)
• Functional Keywords: light-harvesting complex, membrane protein, plant, photosynthesis
• Biological source: Spinacia oleracea (spinach)
• Total number of polymer chains: 10
• Total formula weight: 419135.19

Authors

Liu, Z.,Yan, H.,Wang, K.,Kuang, T.,Zhang, J.,Gui, L.,An, X.,Chang, W. (deposition date: 2003-12-17, release date: 2004-03-30, Last modification date: 2024-03-13)

Primary citation

Liu, Z.,Yan, H.,Wang, K.,Kuang, T.,Zhang, J.,Gui, L.,An, X.,Chang, W.
Crystal structure of spinach major light-harvesting complex at 2.72 A resolution
Nature, 428:287-292, 2004

PubMed Abstract: The major light-harvesting complex of photosystem II (LHC-II) serves as the principal solar energy collector in the photosynthesis of green plants and presumably also functions in photoprotection under high-light conditions. Here we report the first X-ray structure of LHC-II in icosahedral proteoliposome assembly at atomic detail. One asymmetric unit of a large R32 unit cell contains ten LHC-II monomers. The 14 chlorophylls (Chl) in each monomer can be unambiguously distinguished as eight Chla and six Chlb molecules. Assignment of the orientation of the transition dipole moment of each chlorophyll has been achieved. All Chlb are located around the interface between adjacent monomers, and together with Chla they are the basis for efficient light harvesting. Four carotenoid-binding sites per monomer have been observed. The xanthophyll-cycle carotenoid at the monomer-monomer interface may be involved in the non-radiative dissipation of excessive energy, one of the photoprotective strategies that have evolved in plants.

PubMed: 15029188
DOI: 10.1038/nature02373

Experimental method

X-RAY DIFFRACTION (2.72 Å)