5LTA

Crystal structure of the Prp43-ADP-BeF3-U7-RNA complex

Summary for 5LTA

• Entry DOI: 10.2210/pdb5lta/pdb
• Related: 5d0u
• Descriptor: Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43, RNA (5'-R(P*UP*UP*UP*UP*UP*UP*UP*U)-3'), ADENOSINE-5'-DIPHOSPHATE, ... (7 entities in total)
• Functional Keywords: rna helicase, deah-box protein, dhx15, protein-rna complex, protein/rna
• Biological source: Chaetomium thermophilum var. thermophilum DSM 1495; More
• Total number of polymer chains: 2
• Total formula weight: 87149.53

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

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: 28092261
DOI: 10.7554/eLife.21510

Experimental method

X-RAY DIFFRACTION (2.621 Å)