8cnt

Structure of the DEAH-box helicase Prp16 in complex with ADP

spinqualitylabelsall models 8cnt, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8cnt is a 1 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: ADP, MG, P6G Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0S0F9_CHATD Publication Abstract from PubMed DEAH-box helicases play a crucial role in pre-mRNA splicing as they are responsible for major rearrangements of the spliceosome and are involved in various quality-ensuring steps. Prp16 is the driving force during spliceosomal catalysis, remodeling the C state into the C* state. Here, the first crystal structure of Prp16 from Chaetomium thermophilum in complex with ADP is reported at 1.9 A resolution. Comparison with the other spliceosomal DEAH-box helicases Prp2, Prp22 and Prp43 reveals an overall identical domain architecture. The beta-hairpin, which is a structural element of the RecA2 domain, exhibits a unique position, punctuating its flexibility. Analysis of cryo-EM models of spliceosomal complexes containing Prp16 reveals that these models show Prp16 in its nucleotide-free state, rendering the model presented here the first structure of Prp16 in complex with a nucleotide. Crystal structure of Prp16 in complex with ADP.,Garbers TB, Enders M, Neumann P, Ficner R Acta Crystallogr F Struct Biol Commun. 2023 Aug 1;79(Pt 8):200-207. doi: , 10.1107/S2053230X23005721. Epub 2023 Jul 25. PMID:37548918 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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