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Statements

Subject Item
n2:RIV%2F68378050%3A_____%2F12%3A00376532%21RIV13-AV0-68378050
rdf:type
skos:Concept n8:Vysledek
dcterms: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 a solution and a detailed analysis of crystal identified dimer organization distinctive from other members of the GalR/LacI family. 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.
dcterms:title
Structure of the effector-binding domain of the arabinose repressor AraR from Bacillus subtilis Structure of the effector-binding domain of the arabinose repressor AraR from Bacillus subtilis
skos:prefLabel
Structure of the effector-binding domain of the arabinose repressor AraR from Bacillus subtilis Structure of the effector-binding domain of the arabinose repressor AraR from Bacillus subtilis
skos:notation
RIV/68378050:_____/12:00376532!RIV13-AV0-68378050
n8:predkladatel
n9:ico%3A68378050
n3:aktivita
n13:Z n13:P
n3:aktivity
P(ME08016), Z(AV0Z40550506), Z(AV0Z50520514)
n3:cisloPeriodika
2
n3:dodaniDat
n20:2013
n3:domaciTvurceVysledku
n4:2204908 n4:6367593
n3:druhVysledku
n17:J
n3:duvernostUdaju
n14:S
n3:entitaPredkladatele
n15:predkladatel
n3:idSjednocenehoVysledku
171899
n3:idVysledku
RIV/68378050:_____/12:00376532
n3:jazykVysledku
n19:eng
n3:klicovaSlova
repressor; dimerization; effector binding; isothermal titration calorimetry
n3:klicoveSlovo
n5:dimerization n5:repressor n5:isothermal%20titration%20calorimetry n5:effector%20binding
n3:kodStatuVydavatele
DK - Dánské království
n3:kontrolniKodProRIV
[79AB189B244E]
n3:nazevZdroje
Acta Crystallographica Section D-Biological Crystallography
n3:obor
n7:CE
n3:pocetDomacichTvurcuVysledku
2
n3:pocetTvurcuVysledku
7
n3:projekt
n11:ME08016
n3:rokUplatneniVysledku
n20:2012
n3:svazekPeriodika
68
n3:tvurceVysledku
Čermáková, Kateřina Pachl, Petr Otwinowski, Z. Řezáčová, Pavlína Fábry, Milan Procházková, Kateřina Sieglová, Irena
n3:wos
000299469100011
n3:zamer
n12:AV0Z40550506 n12:AV0Z50520514
s:issn
0907-4449
s:numberOfPages
10
n18:doi
10.1107/S090744491105414X