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	Carotenoid assembly regulates quinone diffusion and the reaction center-light harvesting complex architecture.
Journal, issue, pages	Elife, Vol. 12, Year 2023
Publish date	Sep 22, 2023
Authors	Jiyu Xin / Yang Shi / Xin Zhang / Xinyi Yuan / Yueyong Xin / Huimin He / Jiejie Shen / Robert E Blankenship / Xiaoling Xu /
PubMed Abstract	Carotenoid (Car) pigments perform central roles in photosynthesis-related light harvesting (LH), photoprotection, and assembly of functional pigment-protein complexes. However, the relationships ...Carotenoid (Car) pigments perform central roles in photosynthesis-related light harvesting (LH), photoprotection, and assembly of functional pigment-protein complexes. However, the relationships between Car depletion in the LH, assembly of the prokaryotic reaction center (RC)-LH complex, and quinone exchange are not fully understood. Here, we analyzed native RC-LH (nRC-LH) and Car-depleted RC-LH (dRC-LH) complexes in , a chlorosome-less filamentous anoxygenic phototroph that forms the deepest branch of photosynthetic bacteria. Newly identified exterior Cars functioned with the bacteriochlorophyll B800 to block the proposed quinone channel between LHαβ subunits in the nRC-LH, forming a sealed LH ring that was disrupted by transmembrane helices from cytochrome and subunit X to allow quinone shuttling. dRC-LH lacked subunit X, leading to an exposed LH ring with a larger opening, which together accelerated the quinone exchange rate. We also assigned amino acid sequences of subunit X and two hypothetical proteins Y and Z that functioned in forming the quinone channel and stabilizing the RC-LH interactions. This study reveals the structural basis by which Cars assembly regulates the architecture and quinone exchange of bacterial RC-LH complexes. These findings mark an important step forward in understanding the evolution and diversity of prokaryotic photosynthetic apparatus.
External links	Elife / PubMed:37737710 / PubMed Central
Methods	EM (single particle)
Resolution	2.8 - 3.1 Å
Structure data	34838 8hju EMDB-34838, PDB-8hju: Cryo-EM structure of native RC-LH complex from Roseiflexus castenholzii at 10,000 lux Method: EM (single particle) / Resolution: 2.8 Å 34839 8hjv EMDB-34839, PDB-8hjv: Cryo-EM structure of carotenoid-depleted RC-LH complex from Roseiflexus castenholzii at 10,000 lux Method: EM (single particle) / Resolution: 3.1 Å 35988 8j5o EMDB-35988, PDB-8j5o: Cryo-EM structure of native RC-LH complex from Roseiflexus castenholzii at 100lux Method: EM (single particle) / Resolution: 2.9 Å 35989 8j5p EMDB-35989, PDB-8j5p: Cryo-EM structure of native RC-LH complex from Roseiflexus castenholzii at 2,000lux Method: EM (single particle) / Resolution: 3.1 Å
Chemicals	ChemComp-BCL: BACTERIOCHLOROPHYLL A / Bacteriochlorophyll ChemComp-KGD: beta,psi-caroten-4-one ChemComp-BPH: BACTERIOPHEOPHYTIN A / Pheophytin ChemComp-MQE: 2-methyl-3-[(2E,6E,10E,14E,18E,22E,26E,30E,34E,38E)-3,7,11,15,19,23,27,31,35,39,43-undecamethyltetratetraconta-2,6,10,1 ChemComp-PGV: (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE / phospholipidYM / Phosphatidylglycerol ChemComp-FE: Unknown entry / Iron ChemComp-HEM: PROTOPORPHYRIN IX CONTAINING FE / Heme B ChemComp-DGA: DIACYL GLYCEROL / Diglyceride ChemComp-BPB*: BACTERIOPHEOPHYTIN B / Pheophytin
Source	roseiflexus castenholzii dsm 13941 (bacteria)
Keywords	PHOTOSYNTHESIS / RC-LH core complex