5DOQ

The structure of bd oxidase from Geobacillus thermodenitrificans

Summary for 5DOQ

• Entry DOI: 10.2210/pdb5doq/pdb
• Descriptor: Bd-type quinol oxidase subunit I, Bd-type quinol oxidase subunit II, Putative membrane protein, ... (5 entities in total)
• Functional Keywords: bd oxidase, terminal oxidase, oxidoreductase
• Biological source: Geobacillus thermodenitrificans (strain NG80-2); More
• Total number of polymer chains: 3
• Total formula weight: 94810.33

Authors

Safarian, S.,Mueller, H.,Rajendran, C.,Preu, J.,Ovchinnikov, S.,Kusumoto, T.,Hirose, T.,Langer, J.,Sakamoto, J.,Michel, H. (deposition date: 2015-09-11, release date: 2016-05-04, Last modification date: 2024-05-08)

Primary citation

Safarian, S.,Rajendran, C.,Muller, H.,Preu, J.,Langer, J.D.,Ovchinnikov, S.,Hirose, T.,Kusumoto, T.,Sakamoto, J.,Michel, H.
Structure of a bd oxidase indicates similar mechanisms for membrane-integrated oxygen reductases.
Science, 352:583-586, 2016

PubMed Abstract: The cytochrome bd oxidases are terminal oxidases that are present in bacteria and archaea. They reduce molecular oxygen (dioxygen) to water, avoiding the production of reactive oxygen species. In addition to their contribution to the proton motive force, they mediate viability under oxygen-related stress conditions and confer tolerance to nitric oxide, thus contributing to the virulence of pathogenic bacteria. Here we present the atomic structure of the bd oxidase from Geobacillus thermodenitrificans, revealing a pseudosymmetrical subunit fold. The arrangement and order of the heme cofactors support the conclusions from spectroscopic measurements that the cleavage of the dioxygen bond may be mechanistically similar to that in the heme-copper-containing oxidases, even though the structures are completely different.

PubMed: 27126043
DOI: 10.1126/science.aaf2477

Experimental method

X-RAY DIFFRACTION (3.05 Å)