دورية أكاديمية
Structure of the effector-binding domain of the arabinose repressor AraR from Bacillus subtilis
| العنوان: | Structure of the effector-binding domain of the arabinose repressor AraR from Bacillus subtilis |
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| المؤلفون: | Procházková, K. (Kateřina), Čermáková, K. (Kateřina), Pachl, P. (Petr), Sieglová, I. (Irena), Fábry, M. (Milan), Otwinowski, Z., Řezáčová, P. (Pavlína) |
| سنة النشر: | 2012 |
| المجموعة: | The Czech Academy of Sciences: Publication Activity (ASEP) / Akademie věd ČR - Publikační činnost |
| مصطلحات موضوعية: | repressor, dimerization, effector binding, isothermal titration calorimetry |
| الوصف: | Arabinose repressor AraR in Bacillus subtilis negatively controls expression of genes in the metabolic pathway of arabinose containing polysaccharides. The protein is composed of two domains of different phylogenetic origin and function: the N-terminal DNA binding domain belonging to GntR family and the C-terminal effector binding domain, a GalR/LacI family member. We determined the crystal structure of the C-terminal effector-binding domain of AraR in complex with the effector L-arabinose at 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 microM. Effect of L-arabinose on the protein oligomeric state was investigated in a solution and a detailed analysis of crystal identified dimer organization distinctive from other members of the GalR/LacI family. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 0907-4449 |
| العلاقة: | urn:pissn: 0907-4449; http://hdl.handle.net/11104/0006963Test |
| DOI: | 10.1107/S090744491105414X |
| الإتاحة: | https://doi.org/10.1107/S090744491105414XTest http://hdl.handle.net/11104/0006963Test |
| رقم الانضمام: | edsbas.DB26E825 |
| قاعدة البيانات: | BASE |
| تدمد: | 09074449 |
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| DOI: | 10.1107/S090744491105414X |