PDBsum entry 4ljy

Hydrolase

PDB id: 4ljy

Contents

Protein chain

451 a.a.

Ligands

ADP

MRD ×2

Metals

_MG

Waters ×250

PDB id:

4ljy

Name:

Hydrolase

Title:

Crystal structure of RNA splicing effector prp5 in complex with adp

Structure:

Pre-mRNA-processing atp-dependent RNA helicase prp5. Chain: a. Fragment: unp residues 206-698. Engineered: yes

Source:

Saccharomyces cerevisiae. Yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: prp5, rna5, ybr237w, ybr1603. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.95Å R-factor: 0.202 R-free: 0.226

Authors:

Z.-M.Zhang,J.Li,F.Yang,Y.Xu,J.Zhou

Key ref:

Z.M.Zhang et al. (2013). Crystal structure of Prp5p reveals interdomain interactions that impact spliceosome assembly. Cell Rep, 5, 1269-1278. PubMed id: 24290758 DOI: 10.1016/j.celrep.2013.10.047

Date:

05-Jul-13 Release date: 11-Dec-13

Protein chain

P21372  (PRP5_YEAST) -  Pre-mRNA-processing ATP-dependent RNA helicase PRP5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 849 a.a.

Struc: 451 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

DOI no: 10.1016/j.celrep.2013.10.047

Cell Rep 5:1269-1278 (2013)

PubMed id: 24290758

Crystal structure of Prp5p reveals interdomain interactions that impact spliceosome assembly.

Z.M.Zhang, F.Yang, J.Zhang, Q.Tang, J.Li, J.Gu, J.Zhou, Y.Z.Xu.

ABSTRACT

The DEAD-box adenosine triphosphatase (ATPase) Prp5p facilitates U2 small nuclear ribonucleoprotein particle (snRNP) binding to the intron branch site region during spliceosome assembly. We present crystal structures of S. cerevisiae Prp5p alone and in complex with ADP at 2.12 Å and 1.95 Å resolution. The three-dimensional packing of Prp5p subdomains differs strikingly from that so far observed in other DEAD-box proteins: two RecA-like subdomains adopt an "open state" conformation stabilized by extensive interactions involving sequences that flank the two subdomains. This conformation is distinct from that required for ATP hydrolysis. Consistent with this, Prp5p mutations that destabilize interdomain interactions exhibited increased ATPase activity in vitro and inhibited splicing of suboptimal branch site substrates in vivo, whereas restoration of interdomain interactions reversed these effects. We conclude that the Prp5p open state conformation is biologically relevant and that disruption of the interdomain interaction facilitates a large-scale conformational change of Prp5p during U2 snRNP-branch site recognition.