Publication Abstract from PubMed
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.
Solution structure of the E. coli ribosome hibernation promoting factor HPF: Implications for the relationship between structure and function.,Sato A, Watanabe T, Maki Y, Ueta M, Yoshida H, Ito Y, Wada A, Mishima M Biochem Biophys Res Commun. 2009 Nov 27;389(4):580-5. Epub 2009 Sep 10. PMID:19747895[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
