1vea

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Crystal Structure of HutP, an RNA binding antitermination protein

Structural highlights

1vea is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:HBN
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HUTP_BACSU Antiterminator that binds to cis-acting regulatory sequences on the mRNA in the presence of histidine, thereby suppressing transcription termination and activating the hut operon for histidine utilization.[HAMAP-Rule:MF_00779]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
2 reviews cite this structure
Posttranscription Initiation Control of Gene Expression Mediated by Bacterial RNA-Binding Proteins.
Babitzke et al. (2019)
1 more
15 other articles
No citations found

References

  1. ↑ Kumarevel T, Fujimoto Z, Karthe P, Oda M, Mizuno H, Kumar PK. Crystal structure of activated HutP; an RNA binding protein that regulates transcription of the hut operon in Bacillus subtilis. Structure. 2004 Jul;12(7):1269-80. PMID:15242603 doi:http://dx.doi.org/10.1016/j.str.2004.05.005

Contents


PDB ID 1vea

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OCA

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