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

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F12%3A00376532" target="_blank" >RIV/61388963:_____/12:00376532 - isvavai.cz</a>

  • Alternative codes found

    RIV/68378050:_____/12:00376532

  • Result on the web

    <a href="http://dx.doi.org/10.1107/S090744491105414X" target="_blank" >http://dx.doi.org/10.1107/S090744491105414X</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1107/S090744491105414X" target="_blank" >10.1107/S090744491105414X</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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 asolution and a detailed analysis of crystal identified dimer organization distinctive from other members of the GalR/LacI family.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/ME08016" target="_blank" >ME08016: Structural studies of transcriptional regulators of the DeoR and GntR families involved in catabolic repression in Bacillus subtilis.</a><br>

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2012

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Acta Crystallographica Section D-Biological Crystallography

  • ISSN

    0907-4449

  • e-ISSN

  • Volume of the periodical

    68

  • Issue of the periodical within the volume

    2

  • Country of publishing house

    DK - DENMARK

  • Number of pages

    10

  • Pages from-to

    176-185

  • UT code for WoS article

    000299469100011

  • EID of the result in the Scopus database