1AR1

Structure at 2.7 Angstrom Resolution of the Paracoccus Denitrificans two-subunit Cytochrome C Oxidase Complexed with an Antibody Fv Fragment

Summary for 1AR1

• Entry DOI: 10.2210/pdb1ar1/pdb
• Descriptor: CYTOCHROME C OXIDASE, ANTIBODY FV FRAGMENT, COPPER (II) ION, ... (10 entities in total)
• Functional Keywords: complex (oxidoreductase-antibody), electron transport, transmembrane, cytochrome oxidase, antibody complex, complex (oxidoreductase-antibody) complex, complex (oxidoreductase/antibody)
• Biological source: Paracoccus denitrificans; More
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P98002 P08306
• Total number of polymer chains: 4
• Total formula weight: 126661.32

Authors

Ostermeier, C.,Harrenga, A.,Ermler, U.,Michel, H. (deposition date: 1997-08-08, release date: 1998-02-11, Last modification date: 2024-11-13)

Primary citation

Ostermeier, C.,Harrenga, A.,Ermler, U.,Michel, H.
Structure at 2.7 A resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment.
Proc.Natl.Acad.Sci.USA, 94:10547-10553, 1997

PubMed Abstract: The aa3 type cytochrome c oxidase consisting of the core subunits I and II only was isolated from the soil bacterium Paracoccus denitrificans and crystallized as complex with a monoclonal antibody Fv fragment. Crystals could be grown in the presence of a number of different nonionic detergents. However, only undecyl-beta-D-maltoside and cyclohexyl-hexyl-beta-D-maltoside yielded well-ordered crystals suitable for high resolution x-ray crystallographic studies. The crystals belong to space group P212121 and diffract x-rays to at least 2.5 A (1 A = 0.1 nm) resolution using synchrotron radiation. The structure was determined to a resolution of 2.7 A using molecular replacement and refined to a crystallographic R-factor of 20.5% (Rfree = 25.9%). The refined model includes subunits I and II and the 2 chains of the Fv fragment, 2 heme A molecules, 3 copper atoms, and 1 Mg/Mn atom, a new metal (Ca) binding site, 52 tentatively identified water molecules, and 9 detergent molecules. Only four of the water molecules are located in the cytoplasmic half of cytochrome c oxidase. Most of them are near the interface of subunits I and II. Several waters form a hydrogen-bonded cluster, including the heme propionates and the Mg/Mn binding site. The Fv fragment binds to the periplasmic polar domain of subunit II and is critically involved in the formation of the crystal lattice. The crystallization procedure is well reproducible and will allow for the analysis of the structures of mechanistically interesting mutant cytochrome c oxidases.

PubMed: 9380672
DOI: 10.1073/pnas.94.20.10547

Experimental method

X-RAY DIFFRACTION (2.7 Å)