1CRK
MITOCHONDRIAL CREATINE KINASE
1CRK の概要
エントリーDOI | 10.2210/pdb1crk/pdb |
分子名称 | CREATINE KINASE, PHOSPHATE ION (2 entities in total) |
機能のキーワード | transferase, creatine kinase |
由来する生物種 | Gallus gallus (chicken) |
細胞内の位置 | Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side: P11009 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 173797.44 |
構造登録者 | Fritz-Wolf, K.,Schnyder, T.,Wallimann, T.,Kabsch, W. (登録日: 1996-03-08, 公開日: 1997-07-07, 最終更新日: 2024-02-07) |
主引用文献 | Fritz-Wolf, K.,Schnyder, T.,Wallimann, T.,Kabsch, W. Structure of mitochondrial creatine kinase. Nature, 381:341-345, 1996 Cited by 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: 8692275DOI: 10.1038/381341a0 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3 Å) |
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