1vea
From Proteopedia
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'''Crystal Structure of HutP, an RNA binding antitermination protein''' | '''Crystal Structure of HutP, an RNA binding antitermination protein''' | ||
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[[Category: Mizuno, H.]] | [[Category: Mizuno, H.]] | ||
[[Category: Oda, M.]] | [[Category: Oda, M.]] | ||
| - | [[Category: | + | [[Category: Antiterminator]] |
| - | [[Category: | + | [[Category: Hutp]] |
| - | [[Category: | + | [[Category: Regulation of transcription]] |
| - | [[Category: | + | [[Category: Rna binding protein]] |
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Revision as of 09:26, 3 May 2008
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. 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 Sat May 3 12:26:21 2008
