9x4g

Structure Of the KEOPS dimer

spinqualitylabelsall models 9x4g, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9x4g is a 8 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.1Å Ligands: K Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9BL28_CAEEL Publication Abstract from PubMed N(6)-threonylcarbamoyladenosine (t(6)A) at tRNA position 37 is essential for translational fidelity and cellular homeostasis. The multi-subunit KEOPS complex catalyzes t(6)A formation in Archaea and Eukarya. Here we present cryo-EM structures of C. elegans KEOPS in its apo and tRNA-bound states. tRNA binding induces concerted conformational rearrangements, distorting the anticodon loop to project A37 into the Kae1 active site. Kae1 recognizes the conserved G10-C25 pair and 36-UAA-38 motif. Bud32 directly contacts the anticodon and acceptor arms, coupling ATP hydrolysis to t(6)A catalysis in the distant Kae1 active site through long-range conformational changes. Cgi121 enhances catalytic efficiency through cooperative binding with Bud32 and the tRNA 3' CCA. Pcc1 stabilizes the anticodon loop and mediates KEOPS dimerization, enhancing tRNA binding and t(6)A activity. GAMOS-associated mutations cluster at functional hotspots within the KEOPS-tRNA complex. This study provides a structural framework for understanding KEOPS mechanism and its cellular roles. Catalytic and regulatory basis of tRNA t(6)A modification by the KEOPS complex.,Zhou L, Zhang Z, Jin M, Xie D, Wen H, Westhof E, Lei D, Zhang W Nat Commun. 2026 May 15. doi: 10.1038/s41467-026-73296-6. PMID:42140986 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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