Abstract
The structures of the two domains of translational initiation factor IF3 from Bacillus stearothermophilus have been solved by X-ray crystallography using single wavelength anomalous scattering and multiwavelength anomalous diffraction. Each of the two domains has an alpha/beta topology, with an exposed beta-sheet that is reminiscent of several ribosomal and other RNA binding proteins. An alpha-helix that protrudes out from the body of the N-terminal domain towards the C-terminal domain suggests that IF3 consists of two RNA binding domains connected by an alpha-helix and that it may bridge two regions of the ribosome. This represents the first high resolution structural information on a translational initiation factor.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Circular Dichroism
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Crystallography, X-Ray
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Eukaryotic Initiation Factor-3
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Geobacillus stearothermophilus / chemistry
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Models, Molecular
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Molecular Sequence Data
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Peptide Fragments / chemistry
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Peptide Initiation Factors / chemistry*
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Peptide Initiation Factors / genetics
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Protein Conformation*
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Protein Structure, Secondary*
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Sequence Alignment
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Serine Endopeptidases
Substances
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Bacterial Proteins
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Eukaryotic Initiation Factor-3
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Peptide Fragments
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Peptide Initiation Factors
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Serine Endopeptidases
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omptin outer membrane protease