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-Structure paper
タイトル | Structure of the peripheral arm of a minimalistic respiratory complex I. |
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ジャーナル・号・ページ | Structure, Vol. 30, Issue 1, Page 80-94.e4, Year 2022 |
掲載日 | 2022年1月6日 |
![]() | Johannes Schimpf / Sabrina Oppermann / Tatjana Gerasimova / Ana Filipa Santos Seica / Petra Hellwig / Irina Grishkovskaya / Daniel Wohlwend / David Haselbach / Thorsten Friedrich / ![]() ![]() ![]() |
PubMed 要旨 | Respiratory complex I drives proton translocation across energy-transducing membranes by NADH oxidation coupled with (ubi)quinone reduction. In humans, its dysfunction is associated with ...Respiratory complex I drives proton translocation across energy-transducing membranes by NADH oxidation coupled with (ubi)quinone reduction. In humans, its dysfunction is associated with neurodegenerative diseases. The Escherichia coli complex represents the structural minimal form of an energy-converting NADH:ubiquinone oxidoreductase. Here, we report the structure of the peripheral arm of the E. coli complex I consisting of six subunits, the FMN cofactor, and nine iron-sulfur clusters at 2.7 Å resolution obtained by cryo electron microscopy. While the cofactors are in equivalent positions as in the complex from other species, individual subunits are adapted to the absence of supernumerary proteins to guarantee structural stability. The catalytically important subunits NuoC and D are fused resulting in a specific architecture of functional importance. Striking features of the E. coli complex are scrutinized by mutagenesis and biochemical characterization of the variants. Moreover, the arrangement of the subunits sheds light on the unknown assembly of the complex. |
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手法 | EM (単粒子) |
解像度 | 2.73 Å |
構造データ | EMDB-11930: E. coli NADH quinone oxidoreductase hydrophilic arm (CASP target) |
化合物 | ![]() ChemComp-SF4: ![]() ChemComp-FES: ![]() ChemComp-MG: ![]() ChemComp-FMN: ![]() ChemComp-HOH: |
由来 |
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![]() | ELECTRON TRANSPORT / E. coli / respiratory complex I |