3IZZ

Models for ribosome components that are nearest neighbors to the bovine mitochondrial initiation factor2 bound to the E. Coli ribosome

3IZZ の概要

• エントリーDOI: 10.2210/pdb3izz/pdb
• 関連するPDBエントリー: 3IZY
• EMDBエントリー: 1854 1855
• 分子名称: Helix 5, 14, 15 (Small Subunit), Helix 18 (Small Subunit), Helix 44 (Small Subunit), ... (6 entities in total)
• 機能のキーワード: 70s, rna, ribosomal protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 136124.97

構造登録者

Yassin, A.S.,Haque, E.,Datta, P.P.,Elmore, K.,Banavali, N.K.,Spremulli, L.L.,Agrawal, R.K. (登録日: 2011-01-20, 公開日: 2011-03-30, 最終更新日: 2024-02-21)

主引用文献

Yassin, A.S.,Haque, M.E.,Datta, P.P.,Elmore, K.,Banavali, N.K.,Spremulli, L.L.,Agrawal, R.K.
Insertion domain within mammalian mitochondrial translation initiation factor 2 serves the role of eubacterial initiation factor 1.
Proc.Natl.Acad.Sci.USA, 108:3918-3923, 2011

PubMed Abstract: Mitochondria have their own translational machineries for the synthesis of thirteen polypeptide chains that are components of the complexes that participate in the process of oxidative phosphorylation (or ATP generation). Translation initiation in mammalian mitochondria requires two initiation factors, IF2(mt) and IF3(mt), instead of the three that are present in eubacteria. The mammalian IF2(mt) possesses a unique 37 amino acid insertion domain, which is known to be important for the formation of the translation initiation complex. We have obtained a three-dimensional cryoelectron microscopic map of the mammalian IF2(mt) in complex with initiator fMet-tRNA(iMet) and the eubacterial ribosome. We find that the 37 amino acid insertion domain interacts with the same binding site on the ribosome that would be occupied by the eubacterial initiation factor IF1, which is absent in mitochondria. Our finding suggests that the insertion domain of IF2(mt) mimics the function of eubacterial IF1, by blocking the ribosomal aminoacyl-tRNA binding site (A site) at the initiation step.

PubMed: 21368145
DOI: 10.1073/pnas.1017425108

実験手法

ELECTRON MICROSCOPY (10.8 Å)