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 alternative complex III in a supercomplex with cytochrome oxidase.
Journal, issue, pages	Nature, Vol. 557, Issue 7703, Page 123-126, Year 2018
Publish date	Apr 25, 2018
Authors	Chang Sun / Samir Benlekbir / Padmaja Venkatakrishnan / Yuhang Wang / Sangjin Hong / Jonathan Hosler / Emad Tajkhorshid / John L Rubinstein / Robert B Gennis /
PubMed Abstract	Alternative complex III (ACIII) is a key component of the respiratory and/or photosynthetic electron transport chains of many bacteria. Like complex III (also known as the bc complex), ACIII ...Alternative complex III (ACIII) is a key component of the respiratory and/or photosynthetic electron transport chains of many bacteria. Like complex III (also known as the bc complex), ACIII catalyses the oxidation of membrane-bound quinol and the reduction of cytochrome c or an equivalent electron carrier. However, the two complexes have no structural similarity. Although ACIII has eluded structural characterization, several of its subunits are known to be homologous to members of the complex iron-sulfur molybdoenzyme (CISM) superfamily , including the proton pump polysulfide reductase. We isolated the ACIII from Flavobacterium johnsoniae with native lipids using styrene maleic acid copolymer, both as an independent enzyme and as a functional 1:1 supercomplex with an aa-type cytochrome c oxidase (cyt aa). We determined the structure of ACIII to 3.4 Å resolution by cryo-electron microscopy and constructed an atomic model for its six subunits. The structure, which contains a [3Fe-4S] cluster, a [4Fe-4S] cluster and six haem c units, shows that ACIII uses known elements from other electron transport complexes arranged in a previously unknown manner. Modelling of the cyt aa component of the supercomplex revealed that it is structurally modified to facilitate association with ACIII, illustrating the importance of the supercomplex in this electron transport chain. The structure also resolves two of the subunits of ACIII that are anchored to the lipid bilayer with N-terminal triacylated cysteine residues, an important post-translational modification found in numerous prokaryotic membrane proteins that has not previously been observed structurally in a lipid bilayer.
External links	Nature / PubMed:29695868 / PubMed Central
Methods	EM (single particle)
Resolution	3.4 - 3.6 Å
Structure data	7286 6btm EMDB-7286: Cryo-EM density map of Alternative Complex III from Flavobacterium johnsoniae (Wild Type) PDB-6btm: Structure of Alternative Complex III from Flavobacterium johnsoniae (Wild Type) Method: EM (single particle) / Resolution: 3.4 Å EMDB-7447: 3.6-angstrom resolution cryo-EM density map of the Alternative Complex III/ cyt c oxidase supercomplex from Flavobacterium johnsoniae (Wild Type) Method: EM (single particle) / Resolution: 3.6 Å EMDB-7448: 3.6-angstrom resolution cryo-EM density map of the Alternative Complex III from Flavobacterium johnsoniae (Wild Type) Method: EM (single particle) / Resolution: 3.6 Å
Chemicals	ChemComp-HEC: HEME C ChemComp-F3S: FE3-S4 CLUSTER ChemComp-SF4: IRON/SULFUR CLUSTER ChemComp-DKA: DECANOIC ACID ChemComp-FAW: (2S)-3-hydroxypropane-1,2-diyl ditetradecanoate
Source	flavobacterium johnsoniae uw101 (bacteria)
Keywords	MEMBRANE PROTEIN / Electron transport chain / triacylated cysteine / heme c domain / iron-sulfur cluster