2FYH
Solution structure of the 2'-5' RNA ligase-like protein from Pyrococcus furiosus
Summary for 2FYH
| Entry DOI | 10.2210/pdb2fyh/pdb |
| Descriptor | putative integral membrane transport protein (1 entity in total) |
| Functional Keywords | 2'-5' rna ligase-like protein, hxtx motif, pyrococcus furiosus, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, ligase |
| Biological source | Pyrococcus furiosus |
| Total number of polymer chains | 1 |
| Total formula weight | 21860.40 |
| Authors | Okada, K.,Matsuda, T.,Sakamoto, T.,Muto, Y.,Yokoyama, S.,Kanai, A.,Kawai, G.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2006-02-08, release date: 2007-02-20, Last modification date: 2024-05-01) |
| Primary citation | Kanai, A.,Sato, A.,Fukuda, Y.,Okada, K.,Matsuda, T.,Sakamoto, T.,Muto, Y.,Yokoyama, S.,Kawai, G.,Tomita, M. Characterization of a heat-stable enzyme possessing GTP-dependent RNA ligase activity from a hyperthermophilic archaeon, Pyrococcus furiosus Rna, 15:420-431, 2009 Cited by PubMed Abstract: Using an expression protein library of a hyperthermophilic archaeon, Pyrococcus furiosus, we identified a gene (PF0027) that encodes a protein with heat-stable cyclic nucleotide phosphodiesterase (CPDase) activity. The PF0027 gene encoded a 21-kDa protein and an amino acid sequence that showed approximately 27% identity to that of the 2'-5' tRNA ligase protein, ligT (20 kDa), from Escherichia coli. We found that the purified PF0027 protein possessed GTP-dependent RNA ligase activity and that synthetic tRNA halves bearing 2',3'-cyclic phosphate and 5'-OH termini were substrates for the ligation reaction in vitro. GTP hydrolysis was not required for the reaction, and GTPgammaS enhanced the tRNA ligation activity of PF0027 protein, suggesting that the ligation step is regulated by a novel mechanism. In comparison to the strong CPDase activity of the PF0027 protein, the RNA ligase activity itself was quite weak, and the ligation product was unstable during in vitro reaction. Finally, we used NMR to determine the solution structure of the PF0027 protein and discuss the implications of our results in understanding the role of the PF0027 protein. PubMed: 19155324DOI: 10.1261/rna.1122109 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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