Protein or peptide: Fe-S-cluster-containing hydrogenase
Protein or peptide: Polysulphide reductase NrfD
Protein or peptide: ActD
Protein or peptide: Quinol:cytochrome c oxidoreductase monoheme cytochrome subunit
Protein or peptide: ActF
Protein or peptide: ActH
Ligand: HEME C
Ligand: FE3-S4 CLUSTER
Ligand: IRON/SULFUR CLUSTER
Function / homology
Function and homology information
membrane => GO:0016020 / electron transfer activity / heme binding / metal ion binding / plasma membrane Similarity search - Function
Menaquinone reductase, multiheme cytochrome c subunit / NrfD family / Alternative complex III, ActD subunit / MoCo/4Fe-4S cofactor protein extended Tat translocation domain / Polysulphide reductase, NrfD / Alternative complex III, ActD subunit / : / Cytochrome c7-like / Cytochrome c7 and related cytochrome c / Multiheme cytochrome c family profile. ...Menaquinone reductase, multiheme cytochrome c subunit / NrfD family / Alternative complex III, ActD subunit / MoCo/4Fe-4S cofactor protein extended Tat translocation domain / Polysulphide reductase, NrfD / Alternative complex III, ActD subunit / : / Cytochrome c7-like / Cytochrome c7 and related cytochrome c / Multiheme cytochrome c family profile. / Cytochrome C oxidase, cbb3-type, subunit III / Multiheme cytochrome superfamily / 4Fe-4S dicluster domain / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily / 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. / 4Fe-4S ferredoxin-type, iron-sulphur binding domain Similarity search - Domain/homology
Cytochrome c family protein / Fe-S-cluster-containing hydrogenase / Polysulphide reductase NrfD / Uncharacterized protein / Quinol:cytochrome c oxidoreductase monoheme cytochrome subunit / Uncharacterized protein / Uncharacterized protein Similarity search - Component
Journal: Nat Commun / Year: 2018 Title: Structural basis for energy transduction by respiratory alternative complex III. Authors: Joana S Sousa / Filipa Calisto / Julian D Langer / Deryck J Mills / Patrícia N Refojo / Miguel Teixeira / Werner Kühlbrandt / Janet Vonck / Manuela M Pereira / Abstract: Electron transfer in respiratory chains generates the electrochemical potential that serves as energy source for the cell. Prokaryotes can use a wide range of electron donors and acceptors and may ...Electron transfer in respiratory chains generates the electrochemical potential that serves as energy source for the cell. Prokaryotes can use a wide range of electron donors and acceptors and may have alternative complexes performing the same catalytic reactions as the mitochondrial complexes. This is the case for the alternative complex III (ACIII), a quinol:cytochrome c/HiPIP oxidoreductase. In order to understand the catalytic mechanism of this respiratory enzyme, we determined the structure of ACIII from Rhodothermus marinus at 3.9 Å resolution by single-particle cryo-electron microscopy. ACIII presents a so-far unique structure, for which we establish the arrangement of the cofactors (four iron-sulfur clusters and six c-type hemes) and propose the location of the quinol-binding site and the presence of two putative proton pathways in the membrane. Altogether, this structure provides insights into a mechanism for energy transduction and introduces ACIII as a redox-driven proton pump.
History
Deposition
Nov 20, 2017
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Header (metadata) release
Mar 14, 2018
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Map release
May 9, 2018
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Update
Dec 11, 2019
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Current status
Dec 11, 2019
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
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