Crystallization and preliminary X-ray diffraction studies of HutP protein: An RNA-binding protein that regulates the transcription of hut operon in Bacillus subtilis

HutP is an RNA-binding protein and regulates the expression of the histidine utilization (hut) operon in Bacillus subtilis by binding to cis-acting regulatory sequences on hut mRNA. A single point mutant (Val51Ile), which has increased affinity for the regulatory sequences, were purified and crystal...

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Bibliographic Details
Published in:Nucleic Acids Symposium Series 2002-11, Vol.2 (1), p.47-48
Main Authors: Kumarevel, Thirumananseri, Fujimoto, Zui, Oda, Masanao, Nishikawa, Satoshi, Mizuno, Hiroshi, Kumar, Penmetcha K.R.
Format: Article
Language:English
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Summary:HutP is an RNA-binding protein and regulates the expression of the histidine utilization (hut) operon in Bacillus subtilis by binding to cis-acting regulatory sequences on hut mRNA. A single point mutant (Val51Ile), which has increased affinity for the regulatory sequences, were purified and crystallized by the hanging drop vapor diffusion method. The space group was P213 with unit cell dimension a=b=c=95.60 Å resolution, and contain two molecules in the asymmetric unit. A complete MAD data set of 3.0 Å resolution were collected at the LIII edge of Hg.
ISSN:0261-3166
1746-8272
DOI:10.1093/nass/2.1.47