5JPT

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

Summary for 5JPT

• Entry DOI: 10.2210/pdb5jpt/pdb
• Related: 2KX2 2XAU 5D0U
• Descriptor: Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43, CYTIDINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (7 entities in total)
• Functional Keywords: rna helicase, prp43p, deah/rha, hydrolase
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Cellular location: Nucleus: P53131
• Total number of polymer chains: 2
• Total formula weight: 176430.29

Authors

Robert-Paganin, J.,Rety, S.,Leulliot, N. (deposition date: 2016-05-04, release date: 2017-02-22, Last modification date: 2024-01-10)

Primary citation

Robert-Paganin, J.,Halladjian, M.,Blaud, M.,Lebaron, S.,Delbos, L.,Chardon, F.,Capeyrou, R.,Humbert, O.,Henry, Y.,Henras, A.K.,Rety, S.,Leulliot, N.
Functional link between DEAH/RHA helicase Prp43 activation and ATP base binding.
Nucleic Acids Res., 45:1539-1552, 2017

PubMed Abstract: 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.

PubMed: 28180308
DOI: 10.1093/nar/gkw1233

Experimental method

X-RAY DIFFRACTION (2.935 Å)