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1vea
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(New page: 200px<br /><applet load="1vea" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vea, resolution 2.80Å" /> '''Crystal Structure of...)
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Revision as of 02:39, 21 November 2007
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Crystal Structure of HutP, an RNA binding antitermination protein
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
1VEA is a Single protein structure of sequence from Bacillus subtilis with HBN as ligand. 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 Nov 21 04:46:17 2007
