7ose

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cytochrome bd-II type oxidase with bound aurachin D

Structural highlights

7ose is a 6 chain structure with sequence from Escherichia coli BW25113. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3Å
Ligands:0NI, HDD, HEB, UQ8
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

APPC_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 PubMed

Cytochrome 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.

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References

  1. Bekker M, de Vries S, Ter Beek A, Hellingwerf KJ, de Mattos MJ. Respiration of Escherichia coli can be fully uncoupled via the nonelectrogenic terminal cytochrome bd-II oxidase. J Bacteriol. 2009 Sep;191(17):5510-7. doi: 10.1128/JB.00562-09. Epub 2009 Jun 19. PMID:19542282 doi:http://dx.doi.org/10.1128/JB.00562-09
  2. Borisov VB, Murali R, Verkhovskaya ML, Bloch DA, Han H, Gennis RB, Verkhovsky MI. Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode. Proc Natl Acad Sci U S A. 2011 Oct 18;108(42):17320-4. doi:, 10.1073/pnas.1108217108. Epub 2011 Oct 10. PMID:21987791 doi:http://dx.doi.org/10.1073/pnas.1108217108
  3. Sharma P, Hellingwerf KJ, de Mattos MJ, Bekker M. Uncoupling of substrate-level phosphorylation in Escherichia coli during glucose-limited growth. Appl Environ Microbiol. 2012 Oct;78(19):6908-13. doi: 10.1128/AEM.01507-12. Epub , 2012 Jul 27. PMID:22843529 doi:http://dx.doi.org/10.1128/AEM.01507-12
  4. Sturr MG, Krulwich TA, Hicks DB. Purification of a cytochrome bd terminal oxidase encoded by the Escherichia coli app locus from a delta cyo delta cyd strain complemented by genes from Bacillus firmus OF4. J Bacteriol. 1996 Mar;178(6):1742-9. PMID:8626304
  5. 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. Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D. Nat Commun. 2021 Nov 11;12(1):6498. PMID:34764272 doi:10.1038/s41467-021-26835-2

Contents


PDB ID 7ose

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