Ontology highlight
ABSTRACT:
SUBMITTER: Schutz P
PROVIDER: S-EPMC2474498 | biostudies-literature | 2008 Jul
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20080707 28
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 conf ...[more]