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6EAC

Pseudomonas syringae SelO

6EAC の概要
エントリーDOI10.2210/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: 30270044
DOI: 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)
構造検証レポート
Validation report summary of 6eac
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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