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

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 Böttcher () and Thorsten Friedrich ()
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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
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

Nature Communications, 2021, vol. 12, issue 1, 1-11

Abstract: 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.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-26835-2

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DOI: 10.1038/s41467-021-26835-2

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