Structural highlights
Publication Abstract from PubMed
The X-ray crystal structure of ribosome hibernation promoting factor (HPF) from Vibrio cholerae is presented at 2.0 A 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 beta-alpha-beta-beta-beta-alpha 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.
Structure of Vibrio cholerae ribosome hibernation promoting factor.,De Bari H, Berry EA Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Mar 1;69(Pt 3):228-36., doi: 10.1107/S1744309113000961. Epub 2013 Feb 22. PMID:23519794[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ De Bari H, Berry EA. Structure of Vibrio cholerae ribosome hibernation promoting factor. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Mar 1;69(Pt 3):228-36., doi: 10.1107/S1744309113000961. Epub 2013 Feb 22. PMID:23519794 doi:10.1107/S1744309113000961
