X-ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding
Copyright policy )X-ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding
X-ray structures of the universal translation initiation factor IF2/eIF5B have been determined in three states: free enzyme, inactive IF2/eIF5B.GDP, and active IF2/eIF5B.GTP. The "chalice-shaped" enzyme is a GTPase that facilitates ribosomal subunit joining and Met-tRNA(i) binding to ribosomes in all three kingdoms of life. The conserved core of IF2/eIF5B consists of an N-terminal G domain (I) plus an EF-Tu-type beta barrel (II), followed by a novel alpha/beta/alpha-sandwich (III) connected via an alpha helix to a second EF-Tu-type beta barrel (IV). Structural comparisons reveal a molecular lever, which amplifies a modest conformational change in the Switch 2 region of the G domain induced by Mg(2+)/GTP binding over a distance of 90 A from the G domain active center to domain IV. Mechanisms of GTPase function and ribosome binding are discussed.
- Rockefeller University United States
- National Institutes of Health United States
- New York University United States
Models, Molecular, Binding Sites, Guanine, Sequence Homology, Amino Acid, Protein Conformation, Methanococcus, Amino Acid Motifs, Molecular Sequence Data, Crystallography, X-Ray, Guanosine Diphosphate, Protein Structure, Secondary, Protein Structure, Tertiary, Enzyme Activation, Peptide Initiation Factors, Escherichia coli, Amino Acid Sequence, Guanosine Triphosphate, Eukaryotic Initiation Factor-5
Models, Molecular, Binding Sites, Guanine, Sequence Homology, Amino Acid, Protein Conformation, Methanococcus, Amino Acid Motifs, Molecular Sequence Data, Crystallography, X-Ray, Guanosine Diphosphate, Protein Structure, Secondary, Protein Structure, Tertiary, Enzyme Activation, Peptide Initiation Factors, Escherichia coli, Amino Acid Sequence, Guanosine Triphosphate, Eukaryotic Initiation Factor-5
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