2RQL

Solution structure of the E. coli ribosome hibernation promoting factor HPF

2RQL の概要

• エントリーDOI: 10.2210/pdb2rql/pdb
• NMR情報: BMRB: 11077
• 分子名称: Probable sigma-54 modulation protein (1 entity in total)
• 機能のキーワード: ribosome hibernation promoting factor, hpf, ribosome, translation
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10767.25

構造登録者

Sato, A.,Mishima, M. (登録日: 2009-08-13, 公開日: 2010-02-02, 最終更新日: 2024-05-29)

主引用文献

Sato, A.,Watanabe, T.,Maki, Y.,Ueta, M.,Yoshida, H.,Ito, Y.,Wada, A.,Mishima, M.
Solution structure of the E. coli ribosome hibernation promoting factor HPF: Implications for the relationship between structure and function.
Biochem.Biophys.Res.Commun., 389:580-585, 2009

PubMed Abstract: The 70S Escherichia coli ribosome dimerizes to form an inactive 100S ribosome during stationary phase, which is called "ribosome hibernation". The hibernation promoting factor HPF plays a crucial role in 100S ribosome formation. However, YfiA, a known paralog of HPF inhibits 100S formation, although it shares high sequence similarity. Here, we report the first solution structure of HPF as determined by multi-dimensional NMR. HPF adopts betaalphabetabetabetaalpha-fold and the overall structure is similar to YfiA as expected. However, detailed structure comparison based on the determined structure in this study revealed that there are remarkable differences around the C-terminal portion of helix alpha2, which is not predicted by homology modeling. Furthermore, some acidic residues conserved only in HPF are located at the rim of the common basic patch.

PubMed: 19747895
DOI: 10.1016/j.bbrc.2009.09.022

実験手法

SOLUTION NMR