2LKC
Free B.st IF2-G2
Summary for 2LKC
| Entry DOI | 10.2210/pdb2lkc/pdb |
| Related | 2LKD |
| NMR Information | BMRB: 6946 |
| Descriptor | Translation initiation factor IF-2 (1 entity in total) |
| Functional Keywords | translation |
| Biological source | Geobacillus stearothermophilus |
| Cellular location | Cytoplasm: P04766 |
| Total number of polymer chains | 1 |
| Total formula weight | 19524.42 |
| Authors | Wienk, H.,Tishchenko, E.,Belardinelli, R.,Tomaselli, S.,Dongre, R.,Spurio, R.,Folkers, G.E.,Gualerzi, C.O.,Boelens, R. (deposition date: 2011-10-10, release date: 2012-02-15, Last modification date: 2024-05-15) |
| Primary citation | Wienk, H.,Tishchenko, E.,Belardinelli, R.,Tomaselli, S.,Dongre, R.,Spurio, R.,Folkers, G.E.,Gualerzi, C.O.,Boelens, R. Structural Dynamics of Bacterial Translation Initiation Factor IF2. J.Biol.Chem., 287:10922-10932, 2012 Cited by PubMed Abstract: Bacterial translation initiation factor IF2 promotes ribosomal subunit association, recruitment, and binding of fMet-tRNA to the ribosomal P-site and initiation dipeptide formation. Here, we present the solution structures of GDP-bound and apo-IF2-G2 of Bacillus stearothermophilus and provide evidence that this isolated domain binds the 50 S ribosomal subunit and hydrolyzes GTP. Differences between the free and GDP-bound structures of IF2-G2 suggest that domain reorganization within the G2-G3-C1 regions underlies the different structural requirements of IF2 during the initiation process. However, these structural signals are unlikely forwarded from IF2-G2 to the C-terminal fMet-tRNA binding domain (IF2-C2) because the connected IF2-C1 and IF2-C2 modules show completely independent mobility, indicating that the bacterial interdomain connector lacks the rigidity that was found in the archaeal IF2 homolog aIF5B. PubMed: 22308033DOI: 10.1074/jbc.M111.333393 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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