6qp0

Crystal structure of Chaetomium thermophilum Kti12 in complex with ADP-AlF3

spinqualitylabelsall models 6qp0, resolution 2.41Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6qp0 is a 1 chain structure with sequence from Chaetomium thermophilum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.409Å Ligands: ADP, AF3, MES, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0SHI1_CHATD Publication Abstract from PubMed Posttranscriptional RNA modifications occur in all domains of life. Modifications of anticodon bases are of particular importance for ribosomal decoding and proteome homeostasis. The Elongator complex modifies uridines in the wobble position and is highly conserved in eukaryotes. Despite recent insights into Elongator's architecture, the structure and function of its regulatory factor Kti12 have remained elusive. Here, we present the crystal structure of Kti12's nucleotide hydrolase domain trapped in a transition state of ATP hydrolysis. The structure reveals striking similarities to an O-phosphoseryl-tRNA kinase involved in the selenocysteine pathway. Both proteins employ similar mechanisms of tRNA binding and show tRNASec-dependent ATPase activity. In addition, we demonstrate that Kti12 binds directly to Elongator and that ATP hydrolysis is crucial for Elongator to maintain proper tRNA anticodon modification levels in vivo. In summary, our data reveal a hitherto uncharacterized link between two translational control pathways that regulate selenocysteine incorporation and affect ribosomal tRNA selection via specific tRNA modifications. Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator.,Krutyholowa R, Hammermeister A, Zabel R, Abdel-Fattah W, Reinhardt-Tews A, Helm M, Stark MJR, Breunig KD, Schaffrath R, Glatt S Nucleic Acids Res. 2019 Mar 27. pii: 5420542. doi: 10.1093/nar/gkz190. PMID:30916349 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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