6PW0

Cytochrome C oxidase delta 6 mutant

Summary for 6PW0

• Entry DOI: 10.2210/pdb6pw0/pdb
• Related: 2GSM
• Related PRD ID: PRD_900001
• Descriptor: Cytochrome c oxidase subunit 1, MAGNESIUM ION, CALCIUM ION, ... (14 entities in total)
• Functional Keywords: oxidase, proton pumping, electron transfer, membrane protein, oxidoreductase
• Biological source: Rhodobacter sphaeroides 2.4.1; More
• Total number of polymer chains: 4
• Total formula weight: 196410.72

Authors

Liu, J.,Ferguson-Miller, S. (deposition date: 2019-07-21, release date: 2019-11-27, Last modification date: 2024-11-20)

Primary citation

Berg, J.,Liu, J.,Svahn, E.,Ferguson-Miller, S.,Brzezinski, P.
Structural changes at the surface of cytochrome c oxidase alter the proton-pumping stoichiometry.
Biochim Biophys Acta Bioenerg, 1861:148116-148116, 2019

PubMed Abstract: Data from earlier studies showed that minor structural changes at the surface of cytochrome c oxidase, in one of the proton-input pathways (the D pathway), result in dramatically decreased activity and a lower proton-pumping stoichiometry. To further investigate how changes around the D pathway orifice influence functionality of the enzyme, here we modified the nearby C-terminal loop of subunit I of the Rhodobacter sphaeroides cytochrome c oxidase. Removal of 16 residues from this flexible surface loop resulted in a decrease in the proton-pumping stoichiometry to <50% of that of the wild-type enzyme. Replacement of the protonatable residue Glu552, part of the same loop, by an Ala, resulted in a similar decrease in the proton-pumping stoichiometry without loss of the O-reduction activity or changes in the proton-uptake kinetics. The data show that minor structural changes at the orifice of the D pathway, at a distance of ~40 Å from the proton gate of cytochrome c oxidase, may alter the proton-pumping stoichiometry of the enzyme.

PubMed: 31733183
DOI: 10.1016/j.bbabio.2019.148116

Experimental method

X-RAY DIFFRACTION (2.5 Å)