Crystal structure of activated HutP; an RNA binding protein that regulates transcription of the hut operon in Bacillus subtilis

Structure
Thirumananseri KumarevelPenmetcha K R Kumar

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.

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Citations

Sep 30, 2005·Nucleic Acids Research·Thirumananseri KumarevelPenmetcha K R Kumar
Nov 16, 2007·Proteins·Thirumananseri KumarevelShigeyuki Yokoyama
Jun 12, 2013·Journal of Structural Biology·Balasundaresan DhakshnamoorthyPenmetcha K R Kumar
Mar 22, 2014·Biochemical and Biophysical Research Communications·Viswanathan ThiruselvamMondikalipudur Nanjappagounder Ponnuswamy
Apr 6, 2005·Nature Structural & Molecular Biology·Paul Gollnick, Alfred Antson
May 19, 2019·Annual Review of Microbiology·Paul BabitzkeTony Romeo
Jun 6, 2006·Journal of Biochemistry·Subash C B GopinathPenmetcha K R Kumar
Nov 23, 2011·Proceedings of the National Academy of Sciences of the United States of America·Sonia PaytubiMalcolm F White
Jun 1, 2014·Biophysics Reviews·Penmetcha K R Kumar, Hiroshi Mizuno

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