6EAC
Pseudomonas syringae SelO
6EAC の概要
| エントリーDOI | 10.2210/pdb6eac/pdb |
| 分子名称 | SelO, MAGNESIUM ION, CALCIUM ION, ... (9 entities in total) |
| 機能のキーワード | ampylation, selenoprotein, pseudokinase, flipped atp, atypical kinase fold, adenylylation, oxidative stress, selenocysteine, transferase |
| 由来する生物種 | Pseudomonas syringae |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 226332.47 |
| 構造登録者 | Tomchick, D.R.,Tagliabracci, V.S.,Sreelatha, A. (登録日: 2018-08-02, 公開日: 2018-10-03, 最終更新日: 2024-03-13) |
| 主引用文献 | Sreelatha, A.,Yee, S.S.,Lopez, V.A.,Park, B.C.,Kinch, L.N.,Pilch, S.,Servage, K.A.,Zhang, J.,Jiou, J.,Karasiewicz-Urbanska, M.,Lobocka, M.,Grishin, N.V.,Orth, K.,Kucharczyk, R.,Pawlowski, K.,Tomchick, D.R.,Tagliabracci, V.S. Protein AMPylation by an Evolutionarily Conserved Pseudokinase. Cell, 175:809-, 2018 Cited by PubMed Abstract: Approximately 10% of human protein kinases are believed to be inactive and named pseudokinases because they lack residues required for catalysis. Here, we show that the highly conserved pseudokinase selenoprotein-O (SelO) transfers AMP from ATP to Ser, Thr, and Tyr residues on protein substrates (AMPylation), uncovering a previously unrecognized activity for a member of the protein kinase superfamily. The crystal structure of a SelO homolog reveals a protein kinase-like fold with ATP flipped in the active site, thus providing a structural basis for catalysis. SelO pseudokinases localize to the mitochondria and AMPylate proteins involved in redox homeostasis. Consequently, SelO activity is necessary for the proper cellular response to oxidative stress. Our results suggest that AMPylation may be a more widespread post-translational modification than previously appreciated and that pseudokinases should be analyzed for alternative transferase activities. PubMed: 30270044DOI: 10.1016/j.cell.2018.08.046 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.269 Å) |
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