Journal
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Volume 68, Issue -, Pages 176-185Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S090744491105414X
Keywords
repressors; dimerization; effector binding; isothermal titration calorimetry; differential scanning fluorimetry; dimeric interface
Funding
- Ministry of Education of the Czech Republic [ME08016]
- Academy of Sciences of the Czech Republic [AV0Z40550506, AV0Z50520514]
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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 similar to 2.2 angstrom resolution. The l-arabinose binding affinity was characterized by isothermal titration calorimetry and differential scanning fluorimetry; the Kd value was 8.4 +/- 0.4 mu M. The effect of l-arabinose on the protein oligomeric state was investigated in solution and detailed analysis of the similar to crystal identified a dimer organization which is distinctive from that of other members of the GalR/LacI family.
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