Structure of the effector-binding domain of the arabinose repressor AraR from Bacillus subtilis

Kateřina Procházková, Kateřina Čermáková, Petr Pachl, Irena Sieglová, Milan Fábry, Zbyszek Otwinowski, Pavlína Řezáčová

Research output: Contribution to journalArticle

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Abstract

In Bacillus subtilis, the arabinose repressor AraR negatively controls the expression of genes in the metabolic pathway of arabinose-containing polysaccharides. The protein is composed of two domains of different phylogenetic origin and function: an N-terminal DNA-binding domain belonging to the GntR family and a C-terminal effector-binding domain that shows similarity to members of the GalR/LacI family. The crystal structure of the C-terminal effector-binding domain of AraR in complex with the effector L-arabinose has been determined at 2.2 Å resolution. The L-arabinose binding affinity was characterized by isothermal titration calorimetry and differential scanning fluorimetry; the K d value was 8.4 ± 0.4 μM. The effect of L-arabinose on the protein oligomeric state was investigated in solution and detailed analysis of the crystal identified a dimer organization which is distinctive from that of other members of the GalR/LacI family.

Original languageEnglish (US)
Pages (from-to)176-185
Number of pages10
JournalActa Crystallographica Section D: Biological Crystallography
Volume68
Issue number2
DOIs
StatePublished - Feb 1 2012

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Keywords

  • differential scanning fluorimetry
  • dimeric interface
  • dimerization
  • effector binding
  • isothermal titration calorimetry
  • repressors

ASJC Scopus subject areas

  • Structural Biology

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