1FFT

The structure of ubiquinol oxidase from Escherichia coli

Summary for 1FFT

• Entry DOI: 10.2210/pdb1fft/pdb
• Descriptor: UBIQUINOL OXIDASE, COPPER (II) ION, PROTOPORPHYRIN IX CONTAINING FE, ... (7 entities in total)
• Functional Keywords: electron transport, cytochrome oxidase, membrane protein, oxidoreductase
• Biological source: Escherichia coli; More
• Total number of polymer chains: 8
• Total formula weight: 285655.15

Authors

Abramson, J.,Riistama, S.,Larsson, G.,Jasaitis, A.,Svensson-Ek, M.,Puustinen, A.,Iwata, S.,Wikstrom, M. (deposition date: 2000-07-26, release date: 2000-10-18, Last modification date: 2024-02-07)

Primary citation

Abramson, J.,Riistama, S.,Larsson, G.,Jasaitis, A.,Svensson-Ek, M.,Laakkonen, L.,Puustinen, A.,Iwata, S.,Wikstrom, M.
The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site.
Nat.Struct.Biol., 7:910-917, 2000

PubMed Abstract: Cell respiration is catalyzed by the heme-copper oxidase superfamily of enzymes, which comprises cytochrome c and ubiquinol oxidases. These membrane proteins utilize different electron donors through dissimilar access mechanisms. We report here the first structure of a ubiquinol oxidase, cytochrome bo3, from Escherichia coli. The overall structure of the enzyme is similar to those of cytochrome c oxidases; however, the membrane-spanning region of subunit I contains a cluster of polar residues exposed to the interior of the lipid bilayer that is not present in the cytochrome c oxidase. Mutagenesis studies on these residues strongly suggest that this region forms a quinone binding site. A sequence comparison of this region with known quinone binding sites in other membrane proteins shows remarkable similarities. In light of these findings we suggest specific roles for these polar residues in electron and proton transfer in ubiquinol oxidase.

PubMed: 11017202
DOI: 10.1038/82824

Experimental method

X-RAY DIFFRACTION (3.5 Å)