2RQL

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

Summary for 2RQL

• Entry DOI: 10.2210/pdb2rql/pdb
• NMR Information: BMRB: 11077
• Descriptor: Probable sigma-54 modulation protein (1 entity in total)
• Functional Keywords: ribosome hibernation promoting factor, hpf, ribosome, translation
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 10767.25

Authors

Sato, A.,Mishima, M. (deposition date: 2009-08-13, release date: 2010-02-02, Last modification date: 2024-05-29)

Primary citation

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

Experimental method

SOLUTION NMR