3TB6

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

Summary for 3TB6

• Entry DOI: 10.2210/pdb3tb6/pdb
• Descriptor: Arabinose metabolism transcriptional repressor, beta-L-arabinopyranose, GLYCEROL, ... (4 entities in total)
• Functional Keywords: transcription regulation, arabinose binding, dna binding protein
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm (Probable): P96711
• Total number of polymer chains: 2
• Total formula weight: 67264.99

Authors

Rezacova, P.,Prochazkova, K. (deposition date: 2011-08-05, release date: 2012-01-25, Last modification date: 2023-09-13)

Primary citation

Prochazkova, K.,Cermakova, K.,Pachl, P.,Sieglova, I.,Fabry, M.,Otwinowski, Z.,Rezacova, P.
Structure of the effector-binding domain of the arabinose repressor AraR from Bacillus subtilis.
Acta Crystallogr.,Sect.D, 68:176-185, 2012

PubMed 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.

PubMed: 22281747
DOI: 10.1107/S090744491105414X

Experimental method

X-RAY DIFFRACTION (2.21 Å)