PDBsum entry 2xau

Hydrolase

PDB id: 2xau

Contents

Protein chains

745 a.a. *

Ligands

ADP ×2

ACT ×2

GOL ×2

Metals

_MG ×2

_NI ×2

Waters ×1419

* Residue conservation analysis

PDB id:

2xau

Name:

Hydrolase

Title:

Crystal structure of the prp43p deah-box RNA helicase in complex with adp

Structure:

Pre-mRNA-splicing factor atp-dependent RNA helicase prp43. Chain: a, b. Synonym: helicase ja1, deah-box RNA helicase prp43p. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.90Å R-factor: 0.186 R-free: 0.224

Authors:

H.Walbott,S.Mouffok,R.Capeyrou,S.Lebaron,H.Van Tilbeurgh,Y.Henry, N.Leulliot

Key ref:

H.Walbott et al. (2010). Prp43p contains a processive helicase structural architecture with a specific regulatory domain. Embo J, 29, 2194-2204. PubMed id: 20512115

Date:

31-Mar-10 Release date: 09-Jun-10

Protein chains

P53131  (PRP43_YEAST) -  Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 767 a.a.

Struc: 745 a.a.

Enzyme reactions

• Enzyme class: E.C.3.6.4.13 - Rna helicase.
• Reaction: ATP + H2O = ADP + phosphate + H⁺

ATP + H2O = ADP (Bound ligand (Het Group name = ADP) corresponds exactly) + phosphate + H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Embo J 29:2194-2204 (2010)

PubMed id: 20512115

Prp43p contains a processive helicase structural architecture with a specific regulatory domain.

H.Walbott, S.Mouffok, R.Capeyrou, S.Lebaron, O.Humbert, H.van Tilbeurgh, Y.Henry, N.Leulliot.

ABSTRACT

The DEAH/RNA helicase A (RHA) helicase family comprises proteins involved in splicing, ribosome biogenesis and transcription regulation. We report the structure of yeast Prp43p, a DEAH/RHA helicase remarkable in that it functions in both splicing and ribosome biogenesis. Prp43p displays a novel structural architecture with an unforeseen homology with the Ski2-like Hel308 DNA helicase. Together with the presence of a beta-hairpin in the second RecA-like domain, Prp43p contains all the structural elements of a processive helicase. Moreover, our structure reveals that the C-terminal domain contains an oligonucleotide/oligosaccharide-binding (OB)-fold placed at the entrance of the putative nucleic acid cavity. Deletion or mutations of this domain decrease the affinity of Prp43p for RNA and severely reduce Prp43p ATPase activity in the presence of RNA. We also show that this domain constitutes the binding site for the G-patch-containing domain of Pfa1p. We propose that the C-terminal domain, specific to DEAH/RHA helicases, is a central player in the regulation of helicase activity by binding both RNA and G-patch domain proteins.