structural communications
The X-ray crystal structure of ribosome hibernation promoting factor (HPF) from Vibrio cholerae is presented at 2.0 Å resolution. The crystal was phased by two-wavelength MAD using cocrystallized cobalt. The asymmetric unit contained two molecules of HPF linked by four Co atoms. The metal-binding sites observed in the crystal are probably not related to biological function. The structure of HPF has a typical β–α–β–β–β–α fold consistent with previous structures of YfiA and HPF from Escherichia coli. Comparison of the new structure with that of HPF from E. coli bound to the Thermus thermophilus ribosome [Polikanov et al. (2012), Science, 336, 915–918] shows that no significant structural changes are induced in HPF by binding.
Keywords: Vibrio cholerae; ribosome hibernation; hibernation promotion factor; ribosome-binding proteins; stationary phase; cold shock; MAD; cobalt; metal-binding site.
Supporting information
Portable Document Format (PDF) file https://doi.org/10.1107/S1744309113000961/kw5057sup1.pdf |
PDB reference: ribosome hibernation promoting factor, 4hei