4OKQ

Crystal structure of the single-stranded RNA binding protein HutP from Geobacillus thermodenitrificans

Summary for 4OKQ

• Entry DOI: 10.2210/pdb4okq/pdb
• Related: 4OK9
• Descriptor: Hut operon positive regulatory protein, MAGNESIUM ION, HISTIDINE, ... (4 entities in total)
• Functional Keywords: antitermination, single stranded-rna binding protein, rna binding protein
• Biological source: Geobacillus thermodenitrificans NG80-2
• Total number of polymer chains: 2
• Total formula weight: 32966.33

Authors

Thiruselvam, V.,Ponnuswamy, M.N.,Kumarevel, T.S. (deposition date: 2014-01-22, release date: 2014-03-19, Last modification date: 2023-11-08)

Primary citation

Thiruselvam, V.,Sivaraman, P.,Kumarevel, T.,Ponnuswamy, M.N.
Crystal structure of the single-stranded RNA binding protein HutP from Geobacillus thermodenitrificans
Biochem.Biophys.Res.Commun., 446:945-951, 2014

PubMed 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-Mg(2+)) and EDTA (0.5 M) treated ternary complex (HutP-l-histidine-Mg(2+)), solved at 1.9 Å and 2.5 Å 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.

PubMed: 24650662
DOI: 10.1016/j.bbrc.2014.03.036

Experimental method

X-RAY DIFFRACTION (2.5 Å)