Crystal Structure of the Cytochrome bc <sub>1</sub> Complex from Bovine Heart Mitochondria

DOI Web Site 28 Citations
  • Di Xia
    D. Xia, H. Kim, and J. Deisenhofer are in the Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75235, USA. C.-A. Yu, J.-Z. Xia, A. M. Kachurin, L. Zhang, and L. Yu are in the Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.
  • Chang-An Yu
    D. Xia, H. Kim, and J. Deisenhofer are in the Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75235, USA. C.-A. Yu, J.-Z. Xia, A. M. Kachurin, L. Zhang, and L. Yu are in the Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.
  • Hoeon Kim
    D. Xia, H. Kim, and J. Deisenhofer are in the Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75235, USA. C.-A. Yu, J.-Z. Xia, A. M. Kachurin, L. Zhang, and L. Yu are in the Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.
  • Jia-Zhi Xia
    D. Xia, H. Kim, and J. Deisenhofer are in the Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75235, USA. C.-A. Yu, J.-Z. Xia, A. M. Kachurin, L. Zhang, and L. Yu are in the Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.
  • Anatoly M. Kachurin
    D. Xia, H. Kim, and J. Deisenhofer are in the Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75235, USA. C.-A. Yu, J.-Z. Xia, A. M. Kachurin, L. Zhang, and L. Yu are in the Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.
  • Li Zhang
    D. Xia, H. Kim, and J. Deisenhofer are in the Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75235, USA. C.-A. Yu, J.-Z. Xia, A. M. Kachurin, L. Zhang, and L. Yu are in the Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.
  • Linda Yu
    D. Xia, H. Kim, and J. Deisenhofer are in the Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75235, USA. C.-A. Yu, J.-Z. Xia, A. M. Kachurin, L. Zhang, and L. Yu are in the Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.
  • Johann Deisenhofer
    D. Xia, H. Kim, and J. Deisenhofer are in the Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75235, USA. C.-A. Yu, J.-Z. Xia, A. M. Kachurin, L. Zhang, and L. Yu are in the Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.

Abstract

<jats:p> On the basis of x-ray diffraction data to a resolution of 2.9 angstroms, atomic models of most protein components of the bovine cytochrome bc <jats:sub>1</jats:sub> complex were built, including core 1, core 2, cytochrome b, subunit 6, subunit 7, a carboxyl-terminal fragment of cytochrome c <jats:sub>1</jats:sub> , and an amino-terminal fragment of the iron-sulfur protein. The positions of the four iron centers within the bc <jats:sub>1</jats:sub> complex and the binding sites of the two specific respiratory inhibitors antimycin A and myxothiazol were identified. The membrane-spanning region of each bc <jats:sub>1</jats:sub> complex monomer consists of 13 transmembrane helices, eight of which belong to cytochrome b. Closely interacting monomers are arranged as symmetric dimers and form cavities through which the inhibitor binding pockets can be accessed. The proteins core 1 and core 2 are structurally similar to each other and consist of two domains of roughly equal size and identical folding topology. </jats:p>

Journal

  • Science

    Science 277 (5322), 60-66, 1997-07-04

    American Association for the Advancement of Science (AAAS)

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