2RFK
Substrate RNA Positioning in the Archaeal H/ACA Ribonucleoprotein Complex
Summary for 2RFK
| Entry DOI | 10.2210/pdb2rfk/pdb |
| Descriptor | guide RNA 1, guide RNA 2, target RNA, ... (7 entities in total) |
| Functional Keywords | protein-rna complex, archaeal h-aca ribonucleoprotein complex, isomerase, trna processing, ribosome biogenesis, rrna processing, isomerase-rna complex, structural genomics, southeast collaboratory for structural genomics, secsg, psi-2, protein structure initiative, isomerase/rna |
| Biological source | Pyrococcus furiosus More |
| Total number of polymer chains | 6 |
| Total formula weight | 72358.01 |
| Authors | Liang, B.,Xue, S.,Terns, R.M.,Terns, M.P.,Li, H.,Southeast Collaboratory for Structural Genomics (SECSG) (deposition date: 2007-09-30, release date: 2008-02-05, Last modification date: 2024-10-30) |
| Primary citation | Liang, B.,Xue, S.,Terns, R.M.,Terns, M.P.,Li, H. Substrate RNA positioning in the archaeal H/ACA ribonucleoprotein complex. Nat.Struct.Mol.Biol., 14:1189-1195, 2007 Cited by PubMed Abstract: The most complex RNA pseudouridylases are H/ACA ribonucleoprotein particles, which use a guide RNA for substrate capture and four proteins (Cbf5, Nop10, Gar1 and L7Ae/NHP2) for substrate modification. Here we report the three-dimensional structure of a catalytically deficient archaeal enzyme complex (including the guide RNA and three of the four essential proteins) bound to a substrate RNA. Extensive interactions of Cbf5 with one guide-substrate helix and a guide RNA stem shape the forked guide–substrate RNA complex structure and position the substrate in proximity of the Cbf5 catalytic center. Our structural and complementary fluorescence analyses also indicate that precise placement of the target uridine at the active site requires a conformation of the guide–substrate RNA duplex that is brought about by the previously identified concurrent interaction of the guide RNA with L7Ae and a composite Cbf5-Nop10 surface, and further identify a residue that is critical in this process. PubMed: 18059286DOI: 10.1038/nsmb1336 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.87 Å) |
Structure validation
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