2L90
Solution structure of murine myristoylated msrA
2L90 の概要
| エントリーDOI | 10.2210/pdb2l90/pdb |
| NMR情報 | BMRB: 17432 |
| 分子名称 | Peptide methionine sulfoxide reductase, MYRISTIC ACID (2 entities in total) |
| 機能のキーワード | oxidoreductase |
| 由来する生物種 | Mus musculus (mouse) |
| 細胞内の位置 | Isoform 1: Mitochondrion. Isoform 2: Cytoplasm: Q9D6Y7 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 23907.94 |
| 構造登録者 | Gruschus, J.M.,Lim, J.,Piszczek, G.,Levine, R.L.,Tjandra, N. (登録日: 2011-01-27, 公開日: 2012-01-11, 最終更新日: 2024-11-06) |
| 主引用文献 | Lim, J.C.,Gruschus, J.M.,Ghesquiere, B.,Kim, G.,Piszczek, G.,Tjandra, N.,Levine, R.L. Characterization and solution structure of mouse myristoylated methionine sulfoxide reductase A. J.Biol.Chem., 287:25589-25595, 2012 Cited by PubMed Abstract: Methionine sulfoxide reductase A is an essential enzyme in the antioxidant system which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide. The cytosolic form of the enzyme is myristoylated, but it is not known to translocate to membranes, and the function of myristoylation is not established. We compared the biochemical and biophysical properties of myristoylated and nonmyristoylated mouse methionine sulfoxide reductase A. These were almost identical for both forms of the enzyme, except that the myristoylated form reduced methionine sulfoxide in protein much faster than the nonmyristoylated form. We determined the solution structure of the myristoylated protein and found that the myristoyl group lies in a relatively surface exposed "myristoyl nest." We propose that this structure functions to enhance protein-protein interaction. PubMed: 22661718DOI: 10.1074/jbc.M112.368936 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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