6eac | pdb_00006eac

Pseudomonas syringae SelO

spinqualitylabelsall models 6eac, resolution 2.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6eac is a 4 chain structure with sequence from Atcc 19310. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, ANP, CA, CL, EDO, MG, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Protein AMPylation by an Evolutionarily Conserved Pseudokinase.,Sreelatha A, Yee SS, Lopez VA, Park BC, Kinch LN, Pilch S, Servage KA, Zhang J, Jiou J, Karasiewicz-Urbanska M, Lobocka M, Grishin NV, Orth K, Kucharczyk R, Pawlowski K, Tomchick DR, Tagliabracci VS Cell. 2018 Sep 25. pii: S0092-8674(18)31107-3. doi: 10.1016/j.cell.2018.08.046. PMID:30270044 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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