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Functional aspects of the X-ray structure of mitochondrial creatine kinase: A molecular physiology approach

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Abstract

Mitochondrial creatine kinase (Mi-CK) is a central enzyme in energy metabolism of tissues with high and fluctuating energy requirements. In this review, recent progress in the functional and structural characterization of Mi-CK is summarized with special emphasis on the solved X-ray structure of chicken Mib-CK octamer (Fritz-Wolf et al., Nature 381, 341-345, 1996). The new results are discussed in a historical context and related to the characteristics of CK isoforms as known from a large number of biophysical and biochemical studies. Finally, two hypothetical functional aspects of the Mi-CK structure are proposed: (i) putative membrane binding motifs at the top and bottom faces of the octamer and (ii) a possible functional role of the central 20 Å channel.

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Authors and Affiliations

  1. Institute of Cell Biology, Swiss Federal Institute of Technology, ETH, Zürich, Switzerland

    Uwe Schlattner, Michael Forstner, Michael Eder, Olaf Stachowiak & Theo Wallimann

  2. Max-Planck Institut für medizinische Forschung, Abt. Biophysik, Jahnstr. 29, Heidelberg, Germany

    Karin Fritz-Wolf

Authors
  1. Uwe Schlattner
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  2. Michael Forstner
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  3. Michael Eder
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  4. Olaf Stachowiak
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  5. Karin Fritz-Wolf
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  6. Theo Wallimann
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Schlattner, U., Forstner, M., Eder, M. et al. Functional aspects of the X-ray structure of mitochondrial creatine kinase: A molecular physiology approach. Mol Cell Biochem 184, 125–140 (1998). https://doi.org/10.1023/A:1006851330913

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  • DOI: https://doi.org/10.1023/A:1006851330913

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