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	Mechanistic and structural diversity between cytochrome isoforms of .
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 118, Issue 50, Year 2021
Publish date	Dec 14, 2021
Authors	Tamara N Grund / Melanie Radloff / Di Wu / Hojjat G Goojani / Luca F Witte / Wiebke Jösting / Sabine Buschmann / Hannelore Müller / Isam Elamri / Sonja Welsch / Harald Schwalbe / Hartmut Michel / Dirk Bald / Schara Safarian /
PubMed Abstract	The treatment of infectious diseases caused by multidrug-resistant pathogens is a major clinical challenge of the 21st century. The membrane-embedded respiratory cytochrome -type oxygen reductase is ...The treatment of infectious diseases caused by multidrug-resistant pathogens is a major clinical challenge of the 21st century. The membrane-embedded respiratory cytochrome -type oxygen reductase is a critical survival factor utilized by pathogenic bacteria during infection, proliferation and the transition from acute to chronic states. encodes for two cytochrome isoforms that are both involved in respiration under oxygen limited conditions. Mechanistic and structural differences between () and () operon encoded cytochrome variants have remained elusive in the past. Here, we demonstrate that cytochrome - catalyzes oxidation of benzoquinols while possessing additional specificity for naphthoquinones. Our data show that although menaquinol-1 (MK1) is not able to directly transfer electrons onto cytochrome from , it has a stimulatory effect on its oxygen reduction rate in the presence of ubiquinol-1. We further determined cryo-EM structures of cytochrome - to high resolution of 2.1 Å. Our structural insights confirm that the general architecture and substrate accessible pathways are conserved between the two oxidase isoforms, but two notable differences are apparent upon inspection: (i) does not contain a CydH-like subunit, thereby exposing heme to the membrane environment and (ii) the AppB subunit harbors a structural demethylmenaquinone-8 molecule instead of ubiquinone-8 as found in CydB of Our work completes the structural landscape of terminal respiratory oxygen reductases of and suggests that structural and functional properties of the respective oxidases are linked to quinol-pool dependent metabolic adaptations in .
External links	Proc Natl Acad Sci U S A / PubMed:34873041 / PubMed Central
Methods	EM (single particle)
Resolution	2.06 - 2.65 Å
Structure data	13108 7oy2 EMDB-13108, PDB-7oy2: High resolution structure of cytochrome bd-II oxidase from E. coli Method: EM (single particle) / Resolution: 2.06 Å EMDB-13117: High resolution structure of cytochrome bd-II oxidase from E. coli at 2.46 A resolution Method: EM (single particle) / Resolution: 2.46 Å EMDB-13121: High resolution structure of cytochrome bd-II oxidase from E. coli at 2.65 A resolution Method: EM (single particle) / Resolution: 2.65 Å EMDB-13122: High resolution structure of cytochrome bd-II oxidase from E. coli at 2.55 A resolution Method: EM (single particle) / Resolution: 2.55 Å
Chemicals	ChemComp-CDN: CARDIOLIPIN / Cardiolipin ChemComp-DK8: 2-[(2~{E},6~{E},10~{Z},14~{E},18~{E},22~{E},26~{E})-3,7,11,15,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaenyl]naphthalene-1,4-dione ChemComp-POV: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipidYM / POPC ChemComp-HEB: HEME B/C ChemComp-HDD: CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE / Heme ChemComp-OXY: OXYGEN MOLECULE / Oxygen ChemComp-HOH*: WATER / Water
Source	Escherichia coli (strain K12) (bacteria) escherichia coli k-12 (bacteria)
Keywords	OXIDOREDUCTASE / Terminal oxidase High resolution Membrane protein Membrane enzyme Oxygen reductase bd oxidase