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 mycobacterial respiratory complex I.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 120, Issue 13, Page e2214949120, Year 2023
Publish date	Mar 28, 2023
Authors	Yingke Liang / Alicia Plourde / Stephanie A Bueler / Jun Liu / Peter Brzezinski / Siavash Vahidi / John L Rubinstein /
PubMed Abstract	Oxidative phosphorylation, the combined activity of the electron transport chain (ETC) and adenosine triphosphate synthase, has emerged as a valuable target for the treatment of infection by and ...Oxidative phosphorylation, the combined activity of the electron transport chain (ETC) and adenosine triphosphate synthase, has emerged as a valuable target for the treatment of infection by and other mycobacteria. The mycobacterial ETC is highly branched with multiple dehydrogenases transferring electrons to a membrane-bound pool of menaquinone and multiple oxidases transferring electrons from the pool. The proton-pumping type I nicotinamide adenine dinucleotide (NADH) dehydrogenase (Complex I) is found in low abundance in the plasma membranes of mycobacteria in typical in vitro culture conditions and is often considered dispensable. We found that growth of in carbon-limited conditions greatly increased the abundance of Complex I and allowed isolation of a rotenone-sensitive preparation of the enzyme. Determination of the structure of the complex by cryoEM revealed the "orphan" two-component response regulator protein MSMEG_2064 as a subunit of the assembly. MSMEG_2064 in the complex occupies a site similar to the proposed redox-sensing subunit NDUFA9 in eukaryotic Complex I. An apparent purine nucleoside triphosphate within the NuoG subunit resembles the GTP-derived molybdenum cofactor in homologous formate dehydrogenase enzymes. The membrane region of the complex binds acyl phosphatidylinositol dimannoside, a characteristic three-tailed lipid from the mycobacterial membrane. The structure also shows menaquinone, which is preferentially used over ubiquinone by gram-positive bacteria, in two different positions along the quinone channel, comparable to ubiquinone in other structures and suggesting a conserved quinone binding mechanism.
External links	Proc Natl Acad Sci U S A / PubMed:36952383 / PubMed Central
Methods	EM (single particle)
Resolution	2.6 - 2.8 Å
Structure data	27963 8e9g EMDB-27963, PDB-8e9g: Mycobacterial respiratory complex I with both quinone positions modelled Method: EM (single particle) / Resolution: 2.6 Å 27964 8e9h EMDB-27964, PDB-8e9h: Mycobacterial respiratory complex I, fully-inserted quinone Method: EM (single particle) / Resolution: 2.7 Å 27965 8e9i EMDB-27965, PDB-8e9i: Mycobacterial respiratory complex I, semi-inserted quinone Method: EM (single particle) / Resolution: 2.8 Å
Chemicals	ChemComp-SF4: IRON/SULFUR CLUSTER ChemComp-MQ9: MENAQUINONE-9 ChemComp-FES: FE2/S2 (INORGANIC) CLUSTER ChemComp-GTP: GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying moleculeYM ChemComp-ZN: Unknown entry ChemComp-FMN: FLAVIN MONONUCLEOTIDE ChemComp-XP2*: (2R)-3-{[(R)-hydroxy({(1S,2R,3R,4R,5S,6S)-3,4,5-trihydroxy-2-(alpha-D-mannopyranosyloxy)-6-[(6-O-undecanoyl-beta-D-mannopyranosyl)oxy]cyclohexyl}oxy)phosphoryl]oxy}-2-(octanoyloxy)propyl undecanoate
Source	mycolicibacterium smegmatis mc2 155 (bacteria)
Keywords	MEMBRANE PROTEIN / Complex / Oxidative Phosphorylation / NADH-quinone oxidoreductase / Iron-sulfur Protein