1CRK

MITOCHONDRIAL CREATINE KINASE

Summary for 1CRK

• Entry DOI: 10.2210/pdb1crk/pdb
• Descriptor: CREATINE KINASE, PHOSPHATE ION (2 entities in total)
• Functional Keywords: transferase, creatine kinase
• Biological source: Gallus gallus (chicken)
• Cellular location: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side: P11009
• Total number of polymer chains: 4
• Total formula weight: 173797.44

Authors

Fritz-Wolf, K.,Schnyder, T.,Wallimann, T.,Kabsch, W. (deposition date: 1996-03-08, release date: 1997-07-07, Last modification date: 2024-02-07)

Primary citation

Fritz-Wolf, K.,Schnyder, T.,Wallimann, T.,Kabsch, W.
Structure of mitochondrial creatine kinase.
Nature, 381:341-345, 1996

PubMed Abstract: 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.

PubMed: 8692275
DOI: 10.1038/381341a0

Experimental method

X-RAY DIFFRACTION (3 Å)