1TIF
TRANSLATION INITIATION FACTOR 3 N-TERMINAL DOMAIN
Summary for 1TIF
| Entry DOI | 10.2210/pdb1tif/pdb |
| Related | 1TIG |
| Descriptor | TRANSLATION INITIATION FACTOR 3, TRIMETHYL LEAD ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | if3 n-terminal domain, ribosome binding factor |
| Biological source | Geobacillus stearothermophilus |
| Cellular location | Cytoplasm: P03000 |
| Total number of polymer chains | 1 |
| Total formula weight | 9437.82 |
| Authors | Biou, V.,Shu, F.,Ramakrishnan, V. (deposition date: 1995-08-16, release date: 1995-12-07, Last modification date: 2024-02-14) |
| Primary citation | Biou, V.,Shu, F.,Ramakrishnan, V. X-ray crystallography shows that translational initiation factor IF3 consists of two compact alpha/beta domains linked by an alpha-helix. EMBO J., 14:4056-4064, 1995 Cited by PubMed 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. PubMed: 7664745PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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