5lta

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

spinqualitylabelsall models 5lta, resolution 2.62Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5lta is a 2 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.621Å Ligands: ADP, BEF, CAC, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0RY84_CHATD Publication Abstract from PubMed The DEAH-box helicase Prp43 is a key player in pre-mRNA splicing as well as the maturation of rRNAs. The exact modus operandi 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 beta-turn of the RecA1 domain containing the newly identified RF motif. This mechanism is clearly different to those of other RNA helicases. Structural insights into the mechanism of the DEAH-box RNA helicase Prp43.,Tauchert MJ, Fourmann JB, Luhrmann R, Ficner R Elife. 2017 Jan 16;6. pii: e21510. doi: 10.7554/eLife.21510. PMID:28092261 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Helicase 3D structures Pre-mRNA splicing factors 3D structures

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