2VSX

Crystal Structure of a Translation Initiation Complex

Summary for 2VSX

• Entry DOI: 10.2210/pdb2vsx/pdb
• Related: 1FUK 1FUU 1QDE 1QVA 1RF8 2VSX
• Descriptor: ATP-DEPENDENT RNA HELICASE EIF4A, EUKARYOTIC INITIATION FACTOR 4F SUBUNIT P150, ADENOSINE MONOPHOSPHATE (3 entities in total)
• Functional Keywords: acetylation, atp-binding, phosphoprotein, protein biosynthesis, translation regulation, translation initiation, translation/hydrolase, initiation factor, nucleotide-binding, helicase, hydrolase, cytoplasm, rna-binding, translation-hydrolase complex
• Biological source: SACCHAROMYCES CEREVISIAE; More
• Total number of polymer chains: 4
• Total formula weight: 154906.81

Authors

Schutz, P.,Bumann, M.,Oberholzer, A.E.,Bieniossek, C.,Altmann, M.,Trachsel, H.,Baumann, U. (deposition date: 2008-04-30, release date: 2008-06-24, Last modification date: 2023-12-13)

Primary citation

Schutz, P.,Bumann, M.,Oberholzer, A.E.,Bieniossek, C.,Trachsel, H.,Altmann, M.,Baumann, U.
Crystal Structure of the Yeast Eif4A-Eif4G Complex: An RNA-Helicase Controlled by Protein-Protein Interactions.
Proc.Natl.Acad.Sci.USA, 105:9564-, 2008

PubMed Abstract: Translation initiation factors eIF4A and eIF4G form, together with the cap-binding factor eIF4E, the eIF4F complex, which is crucial for recruiting the small ribosomal subunit to the mRNA 5' end and for subsequent scanning and searching for the start codon. eIF4A is an ATP-dependent RNA helicase whose activity is stimulated by binding to eIF4G. We report here the structure of the complex formed by yeast eIF4G's middle domain and full-length eIF4A at 2.6-A resolution. eIF4A shows an extended conformation where eIF4G holds its crucial DEAD-box sequence motifs in a productive conformation, thus explaining the stimulation of eIF4A's activity. A hitherto undescribed interaction involves the amino acid Trp-579 of eIF4G. Mutation to alanine results in decreased binding to eIF4A and a temperature-sensitive phenotype of yeast cells that carry a Trp579Ala mutation as its sole source for eIF4G. Conformational changes between eIF4A's closed and open state provide a model for its RNA-helicase activity.

PubMed: 18606994
DOI: 10.1073/PNAS.0800418105

Experimental method

X-RAY DIFFRACTION (2.8 Å)