4OK9: Crystal Structure Of The Single-stranded Rna Binding Protein Hutp From Geobacillus Thermodenitrificans

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.
PDB ID: 4OK9Download
MMDB ID: 118488
PDB Deposition Date: 2014/1/22
Updated in MMDB: 2014/12
Experimental Method:
x-ray diffraction
Resolution: 1.91  Å
Source Organism:
Similar Structures:
Biological Unit for 4OK9: hexameric; determined by author and by software (PISA)
Molecular Components in 4OK9
Label Count Molecule
Proteins (6 molecules)
HUT Operon Positive Regulatory Protein(Gene symbol: GTNG_RS02065)
Molecule annotation
Chemicals (16 molecules)
* Click molecule labels to explore molecular sequence information.

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