2AK2
ADENYLATE KINASE ISOENZYME-2
2AK2 の概要
エントリーDOI | 10.2210/pdb2ak2/pdb |
分子名称 | ADENYLATE KINASE ISOENZYME-2, SULFATE ION (3 entities in total) |
機能のキーワード | nucleoside monophosphate kinase, phosphotransferase |
由来する生物種 | Bos taurus (cattle) |
細胞内の位置 | Mitochondrion intermembrane space: P08166 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 25636.57 |
構造登録者 | |
主引用文献 | Schlauderer, G.J.,Schulz, G.E. The structure of bovine mitochondrial adenylate kinase: comparison with isoenzymes in other compartments. Protein Sci., 5:434-441, 1996 Cited by PubMed Abstract: In vertebrates, there are different adenylate kinases in the compartments cytosol, mitochondrial intermembrane space, and mitochondrial matrix. Here, we report the spatial structure of the intermembrane species established in two crystal forms by X-ray diffraction analyses at 1.92 and 2.1 A resolution. In both structures, the enzyme is unligated, and thus in an "open" conformation. The enzyme was prepared from bovine liver, containing at least five variants arisen from posttranscriptional and posttranslational modifications. It could only be crystallized after removing some of these variants. A comparison with the known structures of the adenylate kinases from cytosol and mitochondrial matrix reveals structural differences that should play a role in protein targeting because none of these enzymes contains a cleavable signal peptide. A further comparison with adenylate kinases from Gram-positive bacteria showed that the structural Zn2+ ion of these species is replaced by a strictly conserved assembly of hydrogen bonded residues. PubMed: 8868479主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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