PDBsum entry: 1qde

Gene regulation

PDB id: 1qde

Contents

Protein chain

203 a.a. *

Ligands

SO4

Waters ×50

* Residue conservation analysis

PDB id:

1qde

Name:

Gene regulation

Title:

Crystal structure of the atpase domain of translation initiation factor 4a from saccharomyces cerevisiae-the prototype of the dead box protein family

Structure:

Translation initiation factor 4a. Chain: a. Fragment: n-terminal domain, residues 9-232. Synonym: eif4a. Engineered: yes

Source:

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

Resolution:

2.00Å R-factor: 0.214 R-free: 0.266

Authors:

J.Benz,H.Trachsel,U.Baumann

Key ref:

J.Benz et al. (1999). Crystal structure of the ATPase domain of translation initiation factor 4A from Saccharomyces cerevisiae--the prototype of the DEAD box protein family. Structure, 7, 671-679. PubMed id: 10404596 DOI: 10.1016/S0969-2126(99)80088-4

Date:

20-May-99 Release date: 23-May-00

Protein chain

P10081  (IF4A_YEAST) -  ATP-dependent RNA helicase eIF4A

Seq: 395 a.a.

Struc: 203 a.a.

Enzyme reactions

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

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

 Gene Ontology (GO) functional annotation 

• Biochemical function: nucleic acid binding (3 terms)

reference

DOI no: 10.1016/S0969-2126(99)80088-4

Structure 7:671-679 (1999)

PubMed id: 10404596

Crystal structure of the ATPase domain of translation initiation factor 4A from Saccharomyces cerevisiae--the prototype of the DEAD box protein family.

J.Benz, H.Trachsel, U.Baumann.

ABSTRACT

BACKGROUND: Translation initiation factor 4A (elF4A) is the prototype of the DEAD-box family of proteins. DEAD-box proteins are involved in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Energy from ATP hydrolysis is used to perform RNA unwinding during initiation of mRNA translation. The presence of elF4A is required for the 43S preinitiation complex to bind to and scan the mRNA. RESULTS: We present here the crystal structure of the nucleotide-binding domain of elF4A at 2.0 A and the structures with bound adenosinediphosphate and adenosinetriphosphate at 2.2 A and 2.4 A resolution, respectively. The structure of the apo form of the enzyme has been determined by multiple isomorphous replacement. The ATPase domain contains a central seven-stranded beta sheet flanked by nine alpha helices. Despite low sequence homology to the NTPase domains of RNA and DNA helicases, the three-dimensional fold of elF4A is nearly identical to the DNA helicase PcrA of Bacillus stearothermophilus and to the RNA helicase NS3 of hepatitis C virus. CONCLUSIONS: We have determined the crystal structure of the N-terminal domain of the elF4A from yeast as the first structure of a member of the DEAD-box protein family. The complex of the protein with bound ADP and ATP offers insight into the mechanism of ATP hydrolysis and the transfer of energy to unwind RNA. The identical fold of the ATPase domain of the DNA helicase PcrA of B. stearothermophilus and the RNA helicase of hepatitis C virus suggests a common fold for all ATPase domains of DExx- and DEAD-box proteins.

Selected figure(s)

Figure 5.
Figure 5. Stereoview of an overlay of eIF4A(9–232) and PcrA. eIF4A is shown in yellow and PcrA is in blue. The view is identical to that in Figure 2b. The figure was prepared with the program MOLSCRIPT.

The above figure is reprinted by permission from Cell Press: Structure (1999, 7, 671-679) copyright 1999.

Figure was selected by an automated process.