1Z9B
Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2
Summary for 1Z9B
| Entry DOI | 10.2210/pdb1z9b/pdb |
| Related | 1D1N |
| Descriptor | Translation initiation factor IF-2 (1 entity in total) |
| Functional Keywords | protein synthesis translation intiation if2 fmet-trna nmr structure, translation |
| Biological source | Geobacillus stearothermophilus |
| Cellular location | Cytoplasm: P04766 |
| Total number of polymer chains | 1 |
| Total formula weight | 14815.85 |
| Authors | Wienk, H.,Tomaselli, S.,Bernard, C.,Spurio, R.,Picone, D.,Gualerzi, C.O.,Boelens, R. (deposition date: 2005-04-01, release date: 2005-08-30, Last modification date: 2024-05-22) |
| Primary citation | Wienk, H.,Tomaselli, S.,Bernard, C.,Spurio, R.,Picone, D.,Gualerzi, C.O.,Boelens, R. Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2 Protein Sci., 14:2461-2468, 2005 Cited by PubMed Abstract: IF2 is one of three bacterial translation initiation factors that are conserved through all kingdoms of life. It binds the 30S and 50S ribosomal subunits, as well as fMet-tRNAf(Met). After these interactions, fMet-tRNAf(Met) is oriented to the ribosomal P-site where the first amino acid of the nascent polypeptide, formylmethionine, is presented. The C-terminal domain of Bacillus stearothermophilus IF2, which is responsible for recognition and binding of fMet-tRNAf(Met), contains two structured modules. Previously, the solution structure of the most C-terminal module, IF2-C2, has been elucidated by NMR spectroscopy and direct interactions between this subdomain and fMet-tRNAf(Met) were reported. In the present NMR study we have obtained the spectral assignment of the other module of the C-terminal domain (IF2-C1) and determined its solution structure and backbone dynamics. The IF2-C1 core forms a flattened fold consisting of a central four-stranded parallel beta-sheet flanked by three alpha-helices. Although its overall organization resembles that of subdomain III of the archaeal IF2-homolog eIF5B whose crystal structure had previously been reported, some differences of potential functional significance are evident. PubMed: 16081655DOI: 10.1110/ps.051531305 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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