7ose | pdb_00007ose
cytochrome bd-II type oxidase with bound aurachin D
Structural highlights
FunctionAPPC_ECOLI A terminal oxidase that catalyzes quinol-dependent, Na(+)-independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested (PubMed:8626304). Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron.[1] [2] [3] [4] Publication Abstract from PubMedCytochrome bd quinol:O(2) 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 A 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(595) 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. Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D.,Grauel A, Kagi J, Rasmussen T, Makarchuk I, Oppermann S, Moumbock AFA, Wohlwend D, Muller R, Melin F, Gunther S, Hellwig P, Bottcher B, Friedrich T Nat Commun. 2021 Nov 11;12(1):6498. doi: 10.1038/s41467-021-26835-2. PMID:34764272[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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