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The CuA domain of Thermus thermophilus ba3-type cytochrome c oxidase at 1.6 Å resolution

Nature Structural Biology volume 6, pages 509–516 (1999)Cite this article

Abstract

The structure of the CuA-containing, extracellular domain of Thermus thermophilus ba3-type cytochrome c oxidase has been determined to 1.6 Å resolution using multiple X-ray wavelength anomalous dispersion (MAD). The Cu2S2 cluster forms a planar rhombus with a copper–copper distance of 2.51 ± 0.03 Å. X-ray absorption fine-structure (EXAFS) studies show that this distance is unchanged by crystallization. The CuA center is asymmetrical; one copper is tetrahedrally coordinated to two bridging cysteine thiolates, one histidine nitrogen and one methionine sulfur, while the other is trigonally coordinated by the two cysteine thiolates and a histidine nitrogen. Combined sequence–structure alignment of amino acid sequences reveals conserved interactions between cytochrome c oxidase subunits I and II.

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Figure 1: a, Stereo ribbon diagram of Thermus ba3-CuA, with the position of every 10th amino acid labeled.
Figure 2: a, A schematic diagram of the geometry of the Thermus ba3-CuA center.
Figure 3: a, Stereo diagram of the structures of Thermus ba3-CuA (in red), CyoA (in blue), bovine (in yellow) and Paracoccus denitrificans subunit II (in green) overlaid on one another.

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Acknowledgements

The authors thank N. Jourdan for assistance with X-ray data collection, and J.M. Castagnetto for assistance with the metal distance searches. X-ray and EXAFS data collection were performed at SSRL, operated by the Department of Energy, Office of Basic Energy Sciences. The SSRL Biotechnology Program is supported by the National Institutes of Health, National Center for Research Resources, Biomedical Technology Program, and by the Department of Energy, Office of Biological and Environmental Research. The Cambridge Structural Database and the Scripps Metalloprotein Database (http://metallo.scripps.edu) were searched for Cu-O bond distances in small molecules and proteins, respectively. This work was supported by the National Institute of Health.

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  1. Donita Sanders

    Present address: University of Michigan, College of Pharmacy, 428 Church Street, Ann Arbor, Michigan, 48109, USA

Authors and Affiliations

  1. Department of Molecular Biology MB-8, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, 92037, California, USA

    Pamela A. Williams, Enrico A. Stura & Duncan E. McRee

  2. Department of Biochemistry and Molecular Biology, Oregon Graduate Institute, Portland, PO Box 91000, Oregon, 97291, USA

    Ninian J. Blackburn

  3. Department of Biology, Mail Code 0368, University of California at San Diego, La Jolla, 92037, California, USA

    Donita Sanders & James A. Fee

  4. Stanford Synchrotron Radiation Laboratory, Stanford, PO Box 4349, MS 69, 94309, California, USA

    Henry Bellamy

  5. Departement d'Ingenierie et d'Etude des Proteines, BAT 152 C.E.A. / SACLAY, 91191, Gif sur Yvette Cedex, France

    Enrico A. Stura

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Correspondence to James A. Fee or Duncan E. McRee.

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Williams, P., Blackburn, N., Sanders, D. et al. The CuA domain of Thermus thermophilus ba3-type cytochrome c oxidase at 1.6 Å resolution. Nat Struct Mol Biol 6, 509–516 (1999). https://doi.org/10.1038/9274

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