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

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Fritz-Wolf,  Karin
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Schlattner, U., Forstner, M., Eder, M., Stachowiak, O., Fritz-Wolf, K., & Wallimann, T. (1998). Functional aspects of the X-ray structure of mitochondrial creatine kinase: a molecular physiology approach. Molecular and Cellular Biochemistry, 184(1-2), 125-140. doi:10.1023/A:1006851330913.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002B-7767-3
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 A channel.