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Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D

Author

Listed:
  • Antonia Grauel

    (Albert-Ludwigs-Universität Freiburg)

  • Jan Kägi

    (Albert-Ludwigs-Universität Freiburg)

  • Tim Rasmussen

    (Julius-Maximilians-Universität Würzburg)

  • Iryna Makarchuk

    (UMR 7140 CMC, Université de Strasbourg, CNRS)

  • Sabrina Oppermann

    (Albert-Ludwigs-Universität Freiburg)

  • Aurélien F. A. Moumbock

    (Albert-Ludwigs-Universität Freiburg)

  • Daniel Wohlwend

    (Albert-Ludwigs-Universität Freiburg)

  • Rolf Müller

    (Helmholtz Institute for Pharmaceutical Research Saarland
    Helmholtz Centre for Infection Research and Department of Pharmacy at Saarland University)

  • Frederic Melin

    (UMR 7140 CMC, Université de Strasbourg, CNRS)

  • Stefan Günther

    (Albert-Ludwigs-Universität Freiburg)

  • Petra Hellwig

    (UMR 7140 CMC, Université de Strasbourg, CNRS)

  • Bettina Böttcher

    (Julius-Maximilians-Universität Würzburg)

  • Thorsten Friedrich

    (Albert-Ludwigs-Universität Freiburg)

Abstract

Cytochrome bd quinol:O2 oxidoreductases are respiratory terminal oxidases so far only identified in prokaryotes, including several pathogenic bacteria. Escherichia coli contains two bd oxidases of which only the bd-I type is structurally characterized. Here, we report the structure of the Escherichia coli cytochrome bd-II type oxidase with the bound inhibitor aurachin D as obtained by electron cryo-microscopy at 3 Å resolution. The oxidase consists of subunits AppB, C and X that show an architecture similar to that of bd-I. The three heme cofactors are found in AppC, while AppB is stabilized by a structural ubiquinone-8 at the homologous positions. A fourth subunit present in bd-I is lacking in bd-II. Accordingly, heme b595 is exposed to the membrane but heme d embedded within the protein and showing an unexpectedly high redox potential is the catalytically active centre. The structure of the Q-loop is fully resolved, revealing the specific aurachin binding.

Suggested Citation

  • Antonia Grauel & Jan Kägi & Tim Rasmussen & Iryna Makarchuk & Sabrina Oppermann & Aurélien F. A. Moumbock & Daniel Wohlwend & Rolf Müller & Frederic Melin & Stefan Günther & Petra Hellwig & Bettina Bö, 2021. "Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-26835-2
    DOI: 10.1038/s41467-021-26835-2
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    References listed on IDEAS

    as
    1. Adar Sonn-Segev & Katarina Belacic & Tatyana Bodrug & Gavin Young & Ryan T. VanderLinden & Brenda A. Schulman & Johannes Schimpf & Thorsten Friedrich & Phat Vinh Dip & Thomas U. Schwartz & Benedikt Ba, 2020. "Quantifying the heterogeneity of macromolecular machines by mass photometry," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
    2. Weiwei Wang & Yan Gao & Yanting Tang & Xiaoting Zhou & Yuezheng Lai & Shan Zhou & Yuying Zhang & Xiuna Yang & Fengjiang Liu & Luke W. Guddat & Quan Wang & Zihe Rao & Hongri Gong, 2021. "Cryo-EM structure of mycobacterial cytochrome bd reveals two oxygen access channels," Nature Communications, Nature, vol. 12(1), pages 1-8, December.
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