7KJT
KEOPS tRNA modifying sub-complex of archaeal Cgi121 and tRNA
Summary for 7KJT
| Entry DOI | 10.2210/pdb7kjt/pdb |
| Related | 7KJU |
| Descriptor | RNA (70-MER), Regulatory protein Cgi121 (2 entities in total) |
| Functional Keywords | keops, trna, cgi121, rna modifying enzyme, n6-threonylcarbamoyl adenosine, rna binding protein-rna complex, rna binding protein/rna |
| Biological source | Methanocaldococcus jannaschii More |
| Total number of polymer chains | 2 |
| Total formula weight | 41850.74 |
| Authors | Ceccarelli, D.F.,Beenstock, J.,Mao, D.Y.L.,Sicheri, F. (deposition date: 2020-10-26, release date: 2020-12-02, Last modification date: 2025-06-25) |
| Primary citation | Beenstock, J.,Ona, S.M.,Porat, J.,Orlicky, S.,Wan, L.C.K.,Ceccarelli, D.F.,Maisonneuve, P.,Szilard, R.K.,Yin, Z.,Setiaputra, D.,Mao, D.Y.L.,Khan, M.,Raval, S.,Schriemer, D.C.,Bayfield, M.A.,Durocher, D.,Sicheri, F. A substrate binding model for the KEOPS tRNA modifying complex. Nat Commun, 11:6233-6233, 2020 Cited by PubMed Abstract: The KEOPS complex, which is conserved across archaea and eukaryotes, is composed of four core subunits; Pcc1, Kae1, Bud32 and Cgi121. KEOPS is crucial for the fitness of all organisms examined. In humans, pathogenic mutations in KEOPS genes lead to Galloway-Mowat syndrome, an autosomal-recessive disease causing childhood lethality. Kae1 catalyzes the universal and essential tRNA modification N-threonylcarbamoyl adenosine, but the precise roles of all other KEOPS subunits remain an enigma. Here we show using structure-guided studies that Cgi121 recruits tRNA to KEOPS by binding to its 3' CCA tail. A composite model of KEOPS bound to tRNA reveals that all KEOPS subunits form an extended tRNA-binding surface that we have validated in vitro and in vivo to mediate the interaction with the tRNA substrate and its modification. These findings provide a framework for understanding the inner workings of KEOPS and delineate why all KEOPS subunits are essential. PubMed: 33277478DOI: 10.1038/s41467-020-19990-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.34 Å) |
Structure validation
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