1M56

Structure of cytochrome c oxidase from Rhodobactor sphaeroides (Wild Type)

Summary for 1M56

• Entry DOI: 10.2210/pdb1m56/pdb
• Related: 1M57
• Descriptor: CYTOCHROME C OXIDASE, COPPER (II) ION, MAGNESIUM ION, ... (10 entities in total)
• Functional Keywords: membrane protein, oxidoreductase
• Biological source: Rhodobacter sphaeroides; More
• Cellular location: Cell membrane; Multi-pass membrane protein: P33517 Q03736; Membrane; Multi-pass membrane protein (By similarity): P84153
• Total number of polymer chains: 8
• Total formula weight: 269272.74

Authors

Svensson-Ek, M.,Abramson, J.,Larsson, G.,Tornroth, S.,Brezezinski, P.,Iwata, S. (deposition date: 2002-07-08, release date: 2002-08-28, Last modification date: 2024-10-23)

Primary citation

Svensson-Ek, M.,Abramson, J.,Larsson, G.,Tornroth, S.,Brzezinski, P.,Iwata, S.
The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides.
J.Mol.Biol., 321:329-339, 2002

PubMed Abstract: The structure of cytochrome c oxidase from Rhodobacter sphaeroides has been solved at 2.3/2.8A (anisotropic resolution). This high-resolution structure revealed atomic details of a bacterial terminal oxidase including water molecule positions and a potential oxygen pathway, which has not been reported in other oxidase structures. A comparative study of the wild-type and the EQ(I-286) mutant enzyme revealed structural rearrangements around E(I-286) that could be crucial for proton transfer in this enzyme. In the structure of the mutant enzyme, EQ(I-286), which cannot transfer protons during oxygen reduction, the side-chain of Q(I-286) does not have the hydrogen bond to the carbonyl oxygen of M(I-107) that is seen in the wild-type structure. Furthermore, the Q(I-286) mutant has a different arrangement of water molecules and residues in the vicinity of the Q side-chain. These differences between the structures could reflect conformational changes that take place upon deprotonation of E(I-286) during turnover of the wild-type enzyme, which could be part of the proton-pumping machinery of the enzyme.

PubMed: 12144789
DOI: 10.1016/S0022-2836(02)00619-8

Experimental method

X-RAY DIFFRACTION (2.3 Å)