Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10755596 | Biochemical and Biophysical Research Communications | 2014 | 7 Pages |
Abstract
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-Mg2+) and EDTA (0.5Â M) treated ternary complex (HutP-l-histidine-Mg2+), solved at 1.9Â Ã
and 2.5Â Ã
resolutions, respectively, from Geobacillus thermodenitrificans. The addition of 0.5Â 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.
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Authors
Viswanathan Thiruselvam, Padavattan Sivaraman, Thirumananseri Kumarevel, Mondikalipudur Nanjappagounder Ponnuswamy,