6EAC

Pseudomonas syringae SelO

Summary for 6EAC

• Entry DOI: 10.2210/pdb6eac/pdb
• Descriptor: SelO, MAGNESIUM ION, CALCIUM ION, ... (9 entities in total)
• Functional Keywords: ampylation, selenoprotein, pseudokinase, flipped atp, atypical kinase fold, adenylylation, oxidative stress, selenocysteine, transferase
• Biological source: Pseudomonas syringae
• Total number of polymer chains: 4
• Total formula weight: 226332.47

Authors

Tomchick, D.R.,Tagliabracci, V.S.,Sreelatha, A. (deposition date: 2018-08-02, release date: 2018-10-03, Last modification date: 2024-03-13)

Primary citation

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

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

Experimental method

X-RAY DIFFRACTION (2.269 Å)