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Functional aspects of the X-ray structure of mitochondrial creatine kinase: a molecular physiology approach.
Schlattner, U; Forstner, M; Eder, M; Stachowiak, O; Fritz-Wolf, K; Wallimann, T.
Affiliation
  • Schlattner U; Swiss Federal Institute of Technology, Institute of Cell Biology, ETH Zürich.
Mol Cell Biochem ; 184(1-2): 125-40, 1998 Jul.
Article in En | MEDLINE | ID: mdl-9746317
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.
Subject(s)
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Collection: 01-internacional Database: MEDLINE Main subject: Creatine Kinase / Mitochondria Type of study: Prognostic_studies Limits: Animals Language: En Journal: Mol Cell Biochem Year: 1998 Document type: Article
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Collection: 01-internacional Database: MEDLINE Main subject: Creatine Kinase / Mitochondria Type of study: Prognostic_studies Limits: Animals Language: En Journal: Mol Cell Biochem Year: 1998 Document type: Article