4ok9 | pdb_00004ok9

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

spinqualitylabelsall models 4ok9, resolution 1.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ok9 is a 2 chain structure with sequence from Geobacillus thermodenitrificans NG80-2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.91Å Ligands: HIS, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HUTP_GEOTN Antiterminator that binds to cis-acting regulatory sequences on the mRNA in the presence of histidine, thereby suppressing transcription termination and activating the hut operon for histidine utilization (By similarity). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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