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


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.

SUBMITTER: Prochazkova K 

PROVIDER: S-EPMC3337009 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature

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

Procházková Kateřina K   Cermáková Kateřina K   Pachl Petr P   Sieglová Irena I   Fábry Milan M   Otwinowski Zbyszek Z   Rezáčová Pavlína P  

Acta crystallographica. Section D, Biological crystallography 20120117 Pt 2


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  ...[more]

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