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
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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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
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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
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