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  • Title: Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D.
    Author: Grauel A, Kägi J, Rasmussen T, Makarchuk I, Oppermann S, Moumbock AFA, Wohlwend D, Müller R, Melin F, Günther S, Hellwig P, Böttcher B, Friedrich T.
    Journal: Nat Commun; 2021 Nov 11; 12(1):6498. PubMed ID: 34764272.
    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.
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