1crk

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MITOCHONDRIAL CREATINE KINASEMITOCHONDRIAL CREATINE KINASE

Structural highlights

1crk is a 4 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:Creatine kinase, with EC number 2.7.3.2
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KCRS_CHICK] Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Structure of mitochondrial creatine kinase.,Fritz-Wolf K, Schnyder T, Wallimann T, Kabsch W Nature. 1996 May 23;381(6580):341-5. PMID:8692275[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Fritz-Wolf K, Schnyder T, Wallimann T, Kabsch W. Structure of mitochondrial creatine kinase. Nature. 1996 May 23;381(6580):341-5. PMID:8692275 doi:10.1038/381341a0

1crk, resolution 3.00Å

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