5LTK
Crystal structure of the Prp43-ADP-BeF3 complex (in hexagonal space group)
Summary for 5LTK
| Entry DOI | 10.2210/pdb5ltk/pdb |
| Related | 5LTA |
| Descriptor | Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43, ADENOSINE-5'-DIPHOSPHATE, BERYLLIUM TRIFLUORIDE ION, ... (6 entities in total) |
| Functional Keywords | spliceosome, rna helicase, deah-box protein, dhx15, hydrolase |
| Biological source | Chaetomium thermophilum var. thermophilum DSM 1495 |
| Total number of polymer chains | 1 |
| Total formula weight | 82350.97 |
| Authors | Tauchert, M.J.,Ficner, R. (deposition date: 2016-09-06, release date: 2017-01-25, Last modification date: 2024-01-17) |
| Primary citation | Tauchert, M.J.,Fourmann, J.B.,Luhrmann, R.,Ficner, R. Structural insights into the mechanism of the DEAH-box RNA helicase Prp43. Elife, 6:-, 2017 Cited by PubMed Abstract: The DEAH-box helicase Prp43 is a key player in pre-mRNA splicing as well as the maturation of rRNAs. The exact of Prp43 and of all other spliceosomal DEAH-box RNA helicases is still elusive. Here, we report crystal structures of Prp43 complexes in different functional states and the analysis of structure-based mutants providing insights into the unwinding and loading mechanism of RNAs. The Prp43•ATP-analog•RNA complex shows the localization of the RNA inside a tunnel formed by the two RecA-like and C-terminal domains. In the ATP-bound state this tunnel can be transformed into a groove prone for RNA binding by large rearrangements of the C-terminal domains. Several conformational changes between the ATP- and ADP-bound states explain the coupling of ATP hydrolysis to RNA translocation, mainly mediated by a β-turn of the RecA1 domain containing the newly identified RF motif. This mechanism is clearly different to those of other RNA helicases. PubMed: 28092261DOI: 10.7554/eLife.21510 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.241 Å) |
Structure validation
Download full validation report
