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
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Journal
IF	>30 >20 >10 >5 all

Title	Cryo-EM structure of the four-subunit cytochrome complex in styrene maleic acid nanodiscs.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 120, Issue 12, Page e2217922120, Year 2023
Publish date	Mar 21, 2023
Authors	David J K Swainsbury / Frederick R Hawkings / Elizabeth C Martin / Sabina Musiał / Jack H Salisbury / Philip J Jackson / David A Farmer / Matthew P Johnson / C Alistair Siebert / Andrew Hitchcock / C Neil Hunter /
PubMed Abstract	Cytochrome complexes are ubiquinol:cytochrome oxidoreductases, and as such, they are centrally important components of respiratory and photosynthetic electron transfer chains in many species of ...Cytochrome complexes are ubiquinol:cytochrome oxidoreductases, and as such, they are centrally important components of respiratory and photosynthetic electron transfer chains in many species of bacteria and in mitochondria. The minimal complex has three catalytic components, which are cytochrome , cytochrome , and the Rieske iron-sulfur subunit, but the function of mitochondrial cytochrome complexes is modified by up to eight supernumerary subunits. The cytochrome complex from the purple phototrophic bacterium has a single supernumerary subunit called subunit IV, which is absent from current structures of the complex. In this work we use the styrene-maleic acid copolymer to purify the cytochrome complex in native lipid nanodiscs, which retains the labile subunit IV, annular lipids, and natively bound quinones. The catalytic activity of the four-subunit cytochrome complex is threefold higher than that of the complex lacking subunit IV. To understand the role of subunit IV, we determined the structure of the four-subunit complex at 2.9 Å using single particle cryogenic electron microscopy. The structure shows the position of the transmembrane domain of subunit IV, which lies across the transmembrane helices of the Rieske and cytochrome subunits. We observe a quinone at the Q quinone-binding site and show that occupancy of this site is linked to conformational changes in the Rieske head domain during catalysis. Twelve lipids were structurally resolved, making contacts with the Rieske and cytochrome subunits, with some spanning both of the two monomers that make up the dimeric complex.
External links	Proc Natl Acad Sci U S A / PubMed:36913593 / PubMed Central
Methods	EM (single particle)
Resolution	2.9 - 3.75 Å
Structure data	15616 8asi EMDB-15616, PDB-8asi: Four subunit cytochrome b-c1 complex from Rhodobacter sphaeroides in native nanodiscs - consensus refinement in the b-b conformation Method: EM (single particle) / Resolution: 2.9 Å 15617 8asj EMDB-15617, PDB-8asj: Four subunit cytochrome b-c1 complex from Rhodobacter sphaeroides in native nanodiscs - focussed refinement in the b-c conformation Method: EM (single particle) / Resolution: 3.75 Å
Chemicals	ChemComp-FES: FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster ChemComp-PEE: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipidYM / Discrete optimized protein energy ChemComp-HEM: PROTOPORPHYRIN IX CONTAINING FE / Heme B ChemComp-HEC: HEME C / Heme C ChemComp-U10*: UBIQUINONE-10 / Coenzyme Q10
Source	Cereibacter sphaeroides (bacteria) cereibacter sphaeroides 2.4.1 (bacteria)
Keywords	OXIDOREDUCTASE / cyt bc1 complex III membrane protein electron transport quinone cytochrome