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PDBsum entry 2vsx
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Translation/hydrolase
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PDB id
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2vsx
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the yeast eif4a-Eif4g complex: an RNA-Helicase controlled by protein-Protein interactions.
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Authors
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P.Schütz,
M.Bumann,
A.E.Oberholzer,
C.Bieniossek,
H.Trachsel,
M.Altmann,
U.Baumann.
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Ref.
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Proc Natl Acad Sci U S A, 2008,
105,
9564-9569.
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PubMed id
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Abstract
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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.
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