1crk
From Proteopedia
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[[Image:1crk.gif|left|200px]] | [[Image:1crk.gif|left|200px]] | ||
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'''MITOCHONDRIAL CREATINE KINASE''' | '''MITOCHONDRIAL CREATINE KINASE''' | ||
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[[Category: Schnyder, T.]] | [[Category: Schnyder, T.]] | ||
[[Category: Wallimann, T.]] | [[Category: Wallimann, T.]] | ||
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Revision as of 10:02, 2 May 2008
MITOCHONDRIAL CREATINE KINASE
Overview
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.
About this Structure
1CRK is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Structure of mitochondrial creatine kinase., Fritz-Wolf K, Schnyder T, Wallimann T, Kabsch W, Nature. 1996 May 23;381(6580):341-5. PMID:8692275 Page seeded by OCA on Fri May 2 13:02:42 2008