National Center for
4OK9: Crystal Structure Of The Single-stranded Rna Binding Protein Hutp From Geobacillus Thermodenitrificans
Crystal structure of the single-stranded RNA binding protein HutP from Geobacillus thermodenitrificans
Biochem. Biophys. Res. Commun. (2014) 446 p.945-951
RNA binding proteins control gene expression by the attenuation/antitermination mechanism. HutP is an RNA binding antitermination protein. It regulates the expression of hut operon when it binds with RNA by modulating the secondary structure of single-stranded hut mRNA. HutP necessitates the presence of l-histidine and divalent metal ion to bind with RNA. Herein, we report the crystal structures of ternary complex (HutP-l-histidine-Mg(2+)) and EDTA (0.5 M) treated ternary complex (HutP-l-histidine-Mg(2+)), solved at 1.9 A and 2.5 A resolutions, respectively, from Geobacillus thermodenitrificans. The addition of 0.5 M EDTA does not affect the overall metal-ion mediated ternary complex structure and however, the metal ions at the non-specific binding sites are chelated, as evidenced from the results of structural features.