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	Structure of the complex I-like molecule NDH of oxygenic photosynthesis.
Journal, issue, pages	Nature, Vol. 566, Issue 7744, Page 411-414, Year 2019
Publish date	Feb 11, 2019
Authors	Thomas G Laughlin / Andrew N Bayne / Jean-François Trempe / David F Savage / Karen M Davies /
PubMed Abstract	Cyclic electron flow around photosystem I (PSI) is a mechanism by which photosynthetic organisms balance the levels of ATP and NADPH necessary for efficient photosynthesis. NAD(P)H dehydrogenase-like ...Cyclic electron flow around photosystem I (PSI) is a mechanism by which photosynthetic organisms balance the levels of ATP and NADPH necessary for efficient photosynthesis. NAD(P)H dehydrogenase-like complex (NDH) is a key component of this pathway in most oxygenic photosynthetic organisms and is the last large photosynthetic membrane-protein complex for which the structure remains unknown. Related to the respiratory NADH dehydrogenase complex (complex I), NDH transfers electrons originating from PSI to the plastoquinone pool while pumping protons across the thylakoid membrane, thereby increasing the amount of ATP produced per NADP molecule reduced. NDH possesses 11 of the 14 core complex I subunits, as well as several oxygenic-photosynthesis-specific (OPS) subunits that are conserved from cyanobacteria to plants. However, the three core complex I subunits that are involved in accepting electrons from NAD(P)H are notably absent in NDH, and it is therefore not clear how NDH acquires and transfers electrons to plastoquinone. It is proposed that the OPS subunits-specifically NdhS-enable NDH to accept electrons from its electron donor, ferredoxin. Here we report a 3.1 Å structure of the 0.42-MDa NDH complex from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1, obtained by single-particle cryo-electron microscopy. Our maps reveal the structure and arrangement of the principal OPS subunits in the NDH complex, as well as an unexpected cofactor close to the plastoquinone-binding site in the peripheral arm. The location of the OPS subunits supports a role in electron transfer and defines two potential ferredoxin-binding sites at the apex of the peripheral arm. These results suggest that NDH could possess several electron transfer routes, which would serve to maximize plastoquinone reduction and avoid deleterious off-target chemistry of the semi-plastoquinone radical.
External links	Nature / PubMed:30742075
Methods	EM (single particle)
Resolution	3.1 - 3.8 Å
Structure data	0415 6nbq 6nby EMDB-0415, PDB-6nbq: T.elongatus NDH (data-set 1) PDB-6nby: T.elongatus NDH (composite model) Method: EM (single particle) / Resolution: 3.1 Å EMDB-0416: T.elongatus NDH Peripheral Arm Focus Map(data-set 1) Method: EM (single particle) / Resolution: 3.6 Å EMDB-0417: T.elongatus NDH Peripheral Arm Focus Map with NdhS(data-set 1) Method: EM (single particle) / Resolution: 3.7 Å EMDB-0418: T.elongatus NDH Peripheral Arm Focus Map without NdhS(data-set 1) Method: EM (single particle) / Resolution: 3.8 Å EMDB-0419: T.elongatus NDH Peripheral Arm Focus Map with X-cofactor(data-set 1) Method: EM (single particle) / Resolution: 3.3 Å EMDB-0420: T.elongatus NDH Peripheral Arm Focus Map without X-cofactor(data-set 1) Method: EM (single particle) / Resolution: 3.4 Å 0425 6nbx EMDB-0425, PDB-6nbx: T.elongatus NDH (data-set 2) Method: EM (single particle) / Resolution: 3.5 Å
Chemicals	ChemComp-SF4: IRON/SULFUR CLUSTER / Iron–sulfur cluster
Source	thermosynechococcus elongatus bp-1 (bacteria) thermosynechococcus elongatus (strain bp-1) (bacteria)
Keywords	OXIDOREDUCTASE / photosynthesis / bioenergetics / membrane protein complex