2NBG
Structure of the Geobacillus stearothermophilus IF2 G3-subdomain
2NBG の概要
| エントリーDOI | 10.2210/pdb2nbg/pdb |
| NMR情報 | BMRB: 25975 |
| 分子名称 | Translation initiation factor IF-2 (1 entity in total) |
| 機能のキーワード | ribosome, translation initiation, translation |
| 由来する生物種 | Geobacillus stearothermophilus |
| 細胞内の位置 | Cytoplasm: P04766 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 13649.75 |
| 構造登録者 | Dongre, R.,Folkers, G.E.,Gualerzi, C.O.,Boelens, R.,Wienk, H. (登録日: 2016-02-11, 公開日: 2016-07-20, 最終更新日: 2024-05-15) |
| 主引用文献 | Dongre, R.,Folkers, G.E.,Gualerzi, C.O.,Boelens, R.,Wienk, H. A model for the interaction of the G3-subdomain of Geobacillus stearothermophilus IF2 with the 30S ribosomal subunit. Protein Sci., 25:1722-1733, 2016 Cited by PubMed Abstract: Bacterial translation initiation factor IF2 complexed with GTP binds to the 30S ribosomal subunit, promotes ribosomal binding of fMet-tRNA, and favors the joining of the small and large ribosomal subunits yielding a 70S initiation complex ready to enter the translation elongation phase. Within the IF2 molecule subdomain G3, which is believed to play an important role in the IF2-30S interaction, is positioned between the GTP-binding G2 and the fMet-tRNA binding C-terminal subdomains. In this study the solution structure of subdomain G3 of Geobacillus stearothermophilus IF2 has been elucidated. G3 forms a core structure consisting of two β-sheets with each four anti-parallel strands, followed by a C-terminal α-helix. In line with its role as linker between G3 and subdomain C1, this helix has no well-defined orientation but is endowed with a dynamic nature. The structure of the G3 core is that of a typical OB-fold module, similar to that of the corresponding subdomain of Thermus thermophilus IF2, and to that of other known RNA-binding modules such as IF2-C2, IF1 and subdomains II of elongation factors EF-Tu and EF-G. Structural comparisons have resulted in a model that describes the interaction between IF2-G3 and the 30S ribosomal subunit. PubMed: 27364543DOI: 10.1002/pro.2977 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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