Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-EM structures of LHCII in photo-active and photo-protecting states reveal allosteric regulation of light harvesting and excess energy dissipation.
Journal, issue, pages	Nat Plants, Vol. 9, Issue 9, Page 1547-1557, Year 2023
Publish date	Aug 31, 2023
Authors	Meixia Ruan / Hao Li / Ying Zhang / Ruoqi Zhao / Jun Zhang / Yingjie Wang / Jiali Gao / Zhuan Wang / Yumei Wang / Dapeng Sun / Wei Ding / Yuxiang Weng /
PubMed Abstract	The major light-harvesting complex of photosystem II (LHCII) has a dual regulatory function in a process called non-photochemical quenching to avoid the formation of reactive oxygen. LHCII undergoes ...The major light-harvesting complex of photosystem II (LHCII) has a dual regulatory function in a process called non-photochemical quenching to avoid the formation of reactive oxygen. LHCII undergoes reversible conformation transitions to switch between a light-harvesting state for excited-state energy transfer and an energy-quenching state for dissipating excess energy under full sunshine. Here we report cryo-electron microscopy structures of LHCII in membrane nanodiscs, which mimic in vivo LHCII, and in detergent solution at pH 7.8 and 5.4, respectively. We found that, under low pH conditions, the salt bridges at the lumenal side of LHCII are broken, accompanied by the formation of two local α-helices on the lumen side. The formation of α-helices in turn triggers allosterically global protein conformational change, resulting in a smaller crossing angle between transmembrane helices. The fluorescence decay rates corresponding to different conformational states follow the Dexter energy transfer mechanism with a characteristic transition distance of 5.6 Å between Lut1 and Chl612. The experimental observations are consistent with the computed electronic coupling strengths using multistate density function theory.
External links	Nat Plants / PubMed:37653340
Methods	EM (single particle)
Resolution	2.52 - 2.8 Å
Structure data	35782 8iwx EMDB-35782, PDB-8iwx: Cryo-EM structure of unprotonated LHCII in detergent solution at high pH value Method: EM (single particle) / Resolution: 2.59 Å 35783 8iwy EMDB-35783, PDB-8iwy: Cryo-EM structure of protonated LHCII in detergent solution at low pH value Method: EM (single particle) / Resolution: 2.68 Å 35784 8iwz EMDB-35784, PDB-8iwz: Cryo-EM structure of unprotonated LHCII in detergent solution at low pH value Method: EM (single particle) / Resolution: 2.52 Å 35785 8ix0 EMDB-35785, PDB-8ix0: Cryo-EM structure of unprotonated LHCII nanodisc at high pH value Method: EM (single particle) / Resolution: 2.64 Å 35786 8ix1 EMDB-35786, PDB-8ix1: Cryo-EM structure of protonated LHCII nanodisc at low pH value Method: EM (single particle) / Resolution: 2.63 Å 35787 8ix2 EMDB-35787, PDB-8ix2: Cryo-EM structure of unprotonated LHCII nanodisc at low pH value Method: EM (single particle) / Resolution: 2.8 Å
Chemicals	ChemComp-CHL: CHLOROPHYLL B ChemComp-CLA: CHLOROPHYLL A ChemComp-LUT: (3R,3'R,6S)-4,5-DIDEHYDRO-5,6-DIHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL ChemComp-XAT: (3S,5R,6S,3'S,5'R,6'S)-5,6,5',6'-DIEPOXY-5,6,5',6'- TETRAHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL ChemComp-NEX: (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 ChemComp-LHG: 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE / phospholipid*YM
Source	spinacia oleracea (spinach) Spinacia (spinach)
Keywords	PLANT PROTEIN / LHCII / Light-harvesting complex / Photosystem II / Photosynthesis II / PHOTOSYNTHESIS