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TitleStructure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 6498, Year 2021
Publish dateNov 11, 2021
AuthorsAntonia 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 / Thorsten Friedrich /
PubMed AbstractCytochrome bd quinol:O oxidoreductases are respiratory terminal oxidases so far only identified in prokaryotes, including several pathogenic bacteria. Escherichia coli contains two bd oxidases of ...Cytochrome bd quinol:O 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 b 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.
External linksNat Commun / PubMed:34764272 / PubMed Central
MethodsEM (single particle)
Resolution3.0 Å
Structure data

EMDB-13048, PDB-7ose:
cytochrome bd-II type oxidase with bound aurachin D
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-HEB:
HEME B/C

ChemComp-HDD:
CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE

ChemComp-0NI:
Aurachin D

ChemComp-UQ8:
Ubiquinone-8

ChemComp-HOH:
WATER

Source
  • escherichia coli bw25113 (bacteria)
KeywordsMEMBRANE PROTEIN / terminal oxidase / Q-loop / inhibitor binding

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