Structural highlights
Publication Abstract from PubMed
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.
Crystal structure of the single-stranded RNA binding protein HutP from Geobacillus thermodenitrificans.,Thiruselvam V, Sivaraman P, Kumarevel T, Ponnuswamy MN Biochem Biophys Res Commun. 2014 Apr 18;446(4):945-51. doi:, 10.1016/j.bbrc.2014.03.036. Epub 2014 Mar 17. PMID:24650662[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Thiruselvam V, Sivaraman P, Kumarevel T, Ponnuswamy MN. Crystal structure of the single-stranded RNA binding protein HutP from Geobacillus thermodenitrificans. Biochem Biophys Res Commun. 2014 Apr 18;446(4):945-51. doi:, 10.1016/j.bbrc.2014.03.036. Epub 2014 Mar 17. PMID:24650662 doi:http://dx.doi.org/10.1016/j.bbrc.2014.03.036
