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

Journal Article · · Acta Crystallographica. Section D: Biological Crystallography
;  [1]; ;  [1];  [2];  [3];  [1]
  1. Academy of Sciences of the Czech Republic, Flemingovo nam. 2, Prague 6 (Czech Republic)
  2. Academy of Sciences of the Czech Republic, Videnska 1083, Prague 4 (Czech Republic)
  3. UT Southwestern Medical Center, Dallas, Texas (United States)

The crystal structure of the effector-binding domain of the transcriptional repressor AraR from B. subtilis in complex with the effector molecule (l-arabinose) was determined at 2.2 Å resolution. A detailed analysis of the crystal identified a dimer organization that is distinctive from that of other members of the GalR/LacI family. 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{sub 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.

OSTI ID:
22351259
Journal Information:
Acta Crystallographica. Section D: Biological Crystallography, Vol. 68, Issue Pt 2; Other Information: PMCID: PMC3337009; PMID: 22281747; PUBLISHER-ID: dz5240; OAI: oai:pubmedcentral.nih.gov:3337009; Copyright (c) International Union of Crystallography 2012; Country of input: International Atomic Energy Agency (IAEA); ISSN 0907-4449
Country of Publication:
Denmark
Language:
English