2BHW

PEA LIGHT-HARVESTING COMPLEX II AT 2.5 ANGSTROM RESOLUTION

Summary for 2BHW

• Entry DOI: 10.2210/pdb2bhw/pdb
• Related: 1VCR
• Descriptor: CHLOROPHYLL A-B BINDING PROTEIN AB80, (3R,3'R,6'S,9R,9'R,13R,13'S)-4',5'-DIDEHYDRO-5',6',7',8',9,9',10,10',11,11',12,12',13,13',14,14',15,15'-OCTADECAHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL, (1R,3R)-6-{(3E,5E,7E,9E,11E,13E,15E,17E)-18-[(1S,4R,6R)-4-HYDROXY-2,2,6-TRIMETHYL-7-OXABICYCLO[4.1.0]HEPT-1-YL]-3,7,12,16-TETRAMETHYLOCTADECA-1,3,5,7,9,11,13,15,17-NONAENYLIDENE}-1,5,5-TRIMETHYLCYCLOHEXANE-1,3-DIOL, ... (9 entities in total)
• Functional Keywords: lhc-ii, photosynthesis, light-harvesting, membrane protein, chlorophyll, chloroplast, chromophore, membrane, phosphorylation, photosystem i, photosystem ii, plastid, thylakoid, transit peptide, transmembrane
• Biological source: PISUM SATIVUM (GARDEN PEA)
• Total number of polymer chains: 3
• Total formula weight: 124670.39

Authors

Standfuss, J.,Terwisscha van Scheltinga, A.C.,Lamborghini, M.,Kuehlbrandt, W. (deposition date: 2005-01-19, release date: 2006-05-23, Last modification date: 2024-05-01)

Primary citation

Standfuss, J.,Terwisscha Van Scheltinga, A.C.,Lamborghini, M.,Kuehlbrandt, W.
Mechanisms of Photoprotection and Nonphotochemical Quenching in Pea Light-Harvesting Complex at 2.5 A Resolution.
Embo J., 24:919-, 2005

PubMed Abstract: The plant light-harvesting complex of photosystem II (LHC-II) collects and transmits solar energy for photosynthesis in chloroplast membranes and has essential roles in regulation of photosynthesis and in photoprotection. The 2.5 A structure of pea LHC-II determined by X-ray crystallography of stacked two-dimensional crystals shows how membranes interact to form chloroplast grana, and reveals the mutual arrangement of 42 chlorophylls a and b, 12 carotenoids and six lipids in the LHC-II trimer. Spectral assignment of individual chlorophylls indicates the flow of energy in the complex and the mechanism of photoprotection in two close chlorophyll a-lutein pairs. We propose a simple mechanism for the xanthophyll-related, slow component of nonphotochemical quenching in LHC-II, by which excess energy is transferred to a zeaxanthin replacing violaxanthin in its binding site, and dissipated as heat. Our structure shows the complex in a quenched state, which may be relevant for the rapid, pH-induced component of nonphotochemical quenching.

PubMed: 15719016
DOI: 10.1038/SJ.EMBOJ.7600585

Experimental method

X-RAY DIFFRACTION (2.5 Å)