3boy

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spinqualitylabelsall models PDB ID 3boy Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 1.70Å
Ligands:	and
Gene:	hutP (Bacillus subtilis)
Coordinates:	save as pdb, mmCIF, xml

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. This structure supersedes 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 Thu Mar 20 19:00:28 2008