De Bari Heather, Berry Edward A
Biochemistry and Molecular Biology, SUNY Upstate Medical University, 750 E. Adams Avenue, Syracuse, NY 13210, USA.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Mar 1;69(Pt 3):228-36. doi: 10.1107/S1744309113000961. Epub 2013 Feb 22.
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.
本文展示了霍乱弧菌核糖体休眠促进因子（HPF）在2.0 Å分辨率下的X射线晶体结构。该晶体通过使用共结晶钴的双波长多波长反常散射法进行相位确定。不对称单元包含由四个钴原子连接的两个HPF分子。晶体中观察到的金属结合位点可能与生物学功能无关。HPF的结构具有典型的β-α-β-β-β-α折叠，与大肠杆菌中YfiA和HPF的先前结构一致。将新结构与结合嗜热栖热菌核糖体的大肠杆菌HPF结构[波利卡诺夫等人（2012年），《科学》，336，915 - 918]进行比较表明，结合不会在HPF中诱导出显著的结构变化。
