5jpt

CRYSTAL STRUCTURE OF THE PRP43P DEAH-BOX RNA HELICASE IN COMPLEX WITH CDP

spinqualitylabelsall models 5jpt, resolution 2.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5jpt is a 2 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.935Å Ligands: ACT, CDP, GOL, MG, NI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PRP43_YEAST Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. Publication Abstract from PubMed The DEAH box helicase Prp43 is a bifunctional enzyme from the DEAH/RHA helicase family required both for the maturation of ribosomes and for lariat intron release during splicing. It interacts with G-patch domain containing proteins which activate the enzymatic activity of Prp43 in vitro by an unknown mechanism. In this work, we show that the activation by G-patch domains is linked to the unique nucleotide binding mode of this helicase family. The base of the ATP molecule is stacked between two residues, R159 of the RecA1 domain (R-motif) and F357 of the RecA2 domain (F-motif). Using Prp43 F357A mutants or pyrimidine nucleotides, we show that the lack of stacking of the nucleotide base to the F-motif decouples the NTPase and helicase activities of Prp43. In contrast the R159A mutant (R-motif) showed reduced ATPase and helicase activities. We show that the Prp43 R-motif mutant induces the same phenotype as the absence of the G-patch protein Gno1, strongly suggesting that the processing defects observed in the absence of Gno1 result from a failure to activate the Prp43 helicase. Overall we propose that the stacking between the R- and F-motifs and the nucleotide base is important for the activity and regulation of this helicase family. Functional link between DEAH/RHA helicase Prp43 activation and ATP base binding.,Robert-Paganin J, Halladjian M, Blaud M, Lebaron S, Delbos L, Chardon F, Capeyrou R, Humbert O, Henry Y, Henras AK, Rety S, Leulliot N Nucleic Acids Res. 2017 Feb 17;45(3):1539-1552. doi: 10.1093/nar/gkw1233. PMID:28180308 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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