Creatine Kinase

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Crystal Structure of mitochondrial Creatine Kinase complex with phosphate 1crk

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Creatine Kinase (CK, EC 2.7.3.2), an enzyme important for energy metabolism in cells of high and fluctuating energy requirements, catalyses the reversible transfer of a phosphoryl goup from phosphocreatine to ADP. We have solved the structure of the octameric mitochondrial isoform, Mib-CK, which is located in the intermembrane compartment and along the cristae membranes. Mib-CK consumes ATP produced in the mitochondria for the production of phosphocreatine, which is then exported into the cytosol for fast regeneration of ATP by the cytosolic CK isoforms. The octamer has 422 point-group symmetry, and appears as a cube of side length 93 angstrom with a channel 20 angstrom wide extending along the four-fold axis. Positively charged amino acids at the four-fold faces of the octamer possibly interact with negatively charged mitochondrial membranes. Each monomer consists of a small alpha-helical domain and a large domain containing an eight-stranded antiparallel beta-sheet flanked by seven alpha-helices. The conserved residues of the CK family form a compact cluster that covers the active site between the domains.


This shows the beta sheets in black. This shows the alpha helices in blue. This shows the amphipathic alpha helix element along the surface of the protein in pink in a single subunit.

3D structures of creatine kinase3D structures of creatine kinase

Updated on 07-March-2013

Creatine kinase - brainCreatine kinase - brain

3drb, 3dre, 3b6r – hB-CK β chain – human
1qh4 – cB-CK - chicken

Creatine kinase – mitochondriaCreatine kinase – mitochondria

2gl6, 1qk1 – hMIB-CK
1crk – cMIB-CK

Creatine kinase – muscleCreatine kinase – muscle

1i0e – hM-CK
2crk - rM-CK – rabbit
1u6r – rM-CK (mutant)
1vrp – M-CK + creatine derivative – Torpedo californica

Creatine kinase – retinalCreatine kinase – retinal

1g0w – CK - bovine

Reference: Fritz-Wolf K, Schnyder T, Wallimann T, Kabsch W Structure of mitochondrial creatine kinase. Nature. 1996 May 23;381(6580):341-5.

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Student, David Canner, Michal Harel, Alexander Berchansky