1VEA

Crystal Structure of HutP, an RNA binding antitermination protein

Summary for 1VEA

• Entry DOI: 10.2210/pdb1vea/pdb
• Descriptor: Hut operon positive regulatory protein, N-(2-NAPHTHYL)HISTIDINAMIDE (3 entities in total)
• Functional Keywords: hutp, antiterminator, rna binding protein, regulation of transcription
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 32745.43

Authors

Kumarevel, T.S.,Fujimoto, Z.,Karthe, P.,Oda, M.,Mizuno, H.,Kumar, P.K.R. (deposition date: 2004-03-29, release date: 2004-07-20, Last modification date: 2023-12-27)

Primary citation

Kumarevel, T.S.,Fujimoto, Z.,Karthe, P.,Oda, M.,Mizuno, H.,Kumar, P.K.R.
Crystal Structure of Activated HutP; An RNA Binding Protein that Regulates Transcription of the hut Operon in Bacillus subtilis
Structure, 12:1269-1280, 2004

PubMed Abstract: HutP is an L-histidine-activated RNA binding protein that regulates the expression of the histidine utilization (hut) operon in Bacillus subtilis by binding to cis-acting regulatory sequences on the hut mRNA. The crystal structure of HutP complexed with an L-histidine analog showed a novel fold; there are four antiparallel beta strands in the central region of each monomer, with two alpha helices each on the front and back. Two HutP monomers form a dimer, and three dimers are arranged in crystallographic 3-fold symmetry to form a hexamer. A histidine analog was located in between the two monomers of HutP, with the imidazole group of L-histidine hydrogen bonded to Glu81. An activation mechanism is proposed based on the identification of key residues of HutP. The HutP binding region in hut mRNA was defined: it consists of three UAG trinucleotide motifs separated by four spacer nucleotides. Residues of HutP potentially important for RNA binding were identified.

PubMed: 15242603
DOI: 10.1016/j.str.2004.05.005

Experimental method

X-RAY DIFFRACTION (2.8 Å)