1WFX
Crystal Structure of APE0204 from Aeropyrum pernix
Summary for 1WFX
| Entry DOI | 10.2210/pdb1wfx/pdb |
| Descriptor | Probable RNA 2'-phosphotransferase, ZINC ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | rna 2'-phosphotransferase, trna splicing, nad, structural genomics, riken structural genomics/proteomics initiative, rsgi, transferase |
| Biological source | Aeropyrum pernix |
| Total number of polymer chains | 1 |
| Total formula weight | 21640.91 |
| Authors | Kato-Murayama, M.,Bessho, Y.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-05-27, release date: 2004-11-27, Last modification date: 2024-11-13) |
| Primary citation | Kato-Murayama, M.,Bessho, Y.,Shirouzu, M.,Yokoyama, S. Crystal Structure of the RNA 2'-Phosphotransferase from Aeropyrum pernix K1 J.Mol.Biol., 348:295-305, 2005 Cited by PubMed Abstract: In the final step of tRNA splicing, the 2'-phosphotransferase catalyzes the transfer of the extra 2'-phosphate from the precursor-ligated tRNA to NAD. We have determined the crystal structure of the 2'-phosphotransferase protein from Aeropyrum pernix K1 at 2.8 Angstroms resolution. The structure of the 2'-phosphotransferase contains two globular domains (N and C-domains), which form a cleft in the center. The N-domain has the winged helix motif, a subfamily of the helix-turn-helix family, which is shared by many DNA-binding proteins. The C-domain of the 2'-phosphotransferase superimposes well on the NAD-binding fold of bacterial (diphtheria) toxins, which catalyze the transfer of ADP ribose from NAD to target proteins, indicating that the mode of NAD binding by the 2'-phosphotransferase could be similar to that of the bacterial toxins. The conserved basic residues are assembled at the periphery of the cleft and could participate in the enzyme contact with the sugar-phosphate backbones of tRNA. The modes by which the two functional domains recognize the two different substrates are clarified by the present crystal structure of the 2'-phosphotransferase. PubMed: 15811369DOI: 10.1016/j.jmb.2005.02.049 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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