Functional aspects of the X-ray structure of mitochondrial creatine kinase: a molecular physiology approach.
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.
Schlattner
U
U
Swiss Federal Institute of Technology, Institute of Cell Biology, ETH Zürich.
Forstner
M
M
Eder
M
M
Stachowiak
O
O
Fritz-Wolf
K
K
Wallimann
T
T
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites / Q000502:physiology; D002645:Chickens; D003401:Creatine / Q000378:metabolism; D003402:Creatine Kinase / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008928:Mitochondria / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010725:Phosphocreatine / Q000378:metabolism; D011487:Protein Conformation
D010725:Phosphocreatine; D003402:Creatine Kinase; D003401:Creatine