3boy

From Proteopedia

Crystal structure of the HutP antitermination complex bound to the HUT mRNA

Overview

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.

About this Structure

3BOY is a Protein complex structure of sequences from Bacillus subtilis with and as ligands. This structure superseeds the now removed PDB entry 2GZT. Full crystallographic information is available from OCA.

Reference

Crystal structure of activated HutP; an RNA binding protein that regulates transcription of the hut operon in Bacillus subtilis., Kumarevel T, Fujimoto Z, Karthe P, Oda M, Mizuno H, Kumar PK, Structure. 2004 Jul;12(7):1269-80. PMID:15242603

Page seeded by OCA on Wed Jan 23 11:11:47 2008