Literature DB >> 12217662

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

T S Kumarevel1, Z Fujimoto, B Padmanabhan, M Oda, S Nishikawa, H Mizuno, P K R Kumar.   

Abstract

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. HutP and its mutant, which has increased affinity for the regulatory sequences, were purified and crystallized by the hanging-drop vapor diffusion method. The space group was P2(1)3 with unit cell dimensions a=b=c=95.6A for HutP and a=b=c=96.8A for the mutant. Complete data sets of 3.0-A resolution for wild-type HutP and of 2.70-A resolution for the mutant HutP were collected.

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Year:  2002        PMID: 12217662     DOI: 10.1016/s1047-8477(02)00024-2

Source DB:  PubMed          Journal:  J Struct Biol        ISSN: 1047-8477            Impact factor:   2.867


  2 in total

1.  Identification of important chemical groups of the hut mRNA for HutP interactions that regulate the hut operon in Bacillus subtilis.

Authors:  T S Kumarevel; S C B Gopinath; S Nishikawa; H Mizuno; P K R Kumar
Journal:  Nucleic Acids Res       Date:  2004-07-25       Impact factor: 16.971

2.  Characterization of the metal ion binding site in the anti-terminator protein, HutP, of Bacillus subtilis.

Authors:  Thirumananseri Kumarevel; Hiroshi Mizuno; Penmetcha K R Kumar
Journal:  Nucleic Acids Res       Date:  2005-09-28       Impact factor: 16.971

  2 in total

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