2R1G

Coordinates of the thermus thermophilus 30S components neighboring RbfA as obtained by fitting into the CRYO-EM map of A 30S-RBFA complex

2R1G の概要

• エントリーDOI: 10.2210/pdb2r1g/pdb
• 関連するPDBエントリー: 1J5E 2DYJ 2R1C
• EMDBエントリー: 1413
• 分子名称: 16S RIBOSOMAL RNA HELIX 1, 30S ribosomal protein S13, 16S RIBOSOMAL RNA HELIX 18, ... (10 entities in total)
• 機能のキーワード: 30s ribosome maturation protein rbfa, cold shock response protein rbfa, 30s-rbfa complex, rbfa binding site on the 30s, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, trna-binding, antibiotic resistance, ribosomal protein-rna complex, ribosomal protein/rna
• 由来する生物種: Thermus thermophilus; 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 100468.52

構造登録者

Datta, P.P.,Wilson, D.N.,Kawazoe, M.,Swami, N.K.,Kaminishi, T.,Sharma, M.R.,Booth, T.M.,Takemoto, C.,Fucini, P.,Yokoyama, S.,Agrawal, R.K. (登録日: 2007-08-22, 公開日: 2008-03-18, 最終更新日: 2024-03-13)

主引用文献

Datta, P.P.,Wilson, D.N.,Kawazoe, M.,Swami, N.K.,Kaminishi, T.,Sharma, M.R.,Booth, T.M.,Takemoto, C.,Fucini, P.,Yokoyama, S.,Agrawal, R.K.
Structural aspects of RbfA action during small ribosomal subunit assembly.
Mol.Cell, 28:434-445, 2007

PubMed Abstract: Ribosome binding factor A (RbfA) is a bacterial cold shock response protein, required for an efficient processing of the 5' end of the 16S ribosomal RNA (rRNA) during assembly of the small (30S) ribosomal subunit. Here we present a crystal structure of Thermus thermophilus (Tth) RbfA and a three-dimensional cryo-electron microscopic (EM) map of the Tth 30S*RbfA complex. RbfA binds to the 30S subunit in a position overlapping the binding sites of the A and P site tRNAs, and RbfA's functionally important C terminus extends toward the 5' end of the 16S rRNA. In the presence of RbfA, a portion of the 16S rRNA encompassing helix 44, which is known to be directly involved in mRNA decoding and tRNA binding, is displaced. These results shed light on the role played by RbfA during maturation of the 30S subunit, and also indicate how RbfA provides cells with a translational advantage under conditions of cold shock.

PubMed: 17996707
DOI: 10.1016/j.molcel.2007.08.026

実験手法

ELECTRON MICROSCOPY (12.5 Å)