-
Something wrong with this record ?
Structure of the effector-binding domain of the arabinose repressor AraR from Bacillus subtilis
K. Procházková, K. Cermáková, P. Pachl, I. Sieglová, M. Fábry, Z. Otwinowski, P. Rezáčová,
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Arabinose metabolism MeSH
- Bacillus subtilis chemistry metabolism MeSH
- Bacterial Proteins chemistry metabolism MeSH
- Crystallography, X-Ray MeSH
- Models, Molecular MeSH
- Repressor Proteins chemistry metabolism MeSH
- Protein Structure, Tertiary MeSH
- Protein Binding MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
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.
References provided by Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc12024086
- 003
- CZ-PrNML
- 005
- 20170410103618.0
- 007
- ta
- 008
- 120815s2012 xxu f 000 0#eng||
- 009
- AR
- 024 7_
- $a 10.1107/s090744491105414x $2 doi
- 035 __
- $a (PubMed)22281747
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a xxu
- 100 1_
- $a Procházková, Kateřina $u Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo nam. 2, Prague 6, Czech Republic.
- 245 10
- $a Structure of the effector-binding domain of the arabinose repressor AraR from Bacillus subtilis / $c K. Procházková, K. Cermáková, P. Pachl, I. Sieglová, M. Fábry, Z. Otwinowski, P. Rezáčová,
- 520 9_
- $a 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.
- 650 _2
- $a arabinosa $x metabolismus $7 D001089
- 650 _2
- $a Bacillus subtilis $x chemie $x metabolismus $7 D001412
- 650 _2
- $a bakteriální proteiny $x chemie $x metabolismus $7 D001426
- 650 _2
- $a krystalografie rentgenová $7 D018360
- 650 _2
- $a molekulární modely $7 D008958
- 650 _2
- $a vazba proteinů $7 D011485
- 650 _2
- $a terciární struktura proteinů $7 D017434
- 650 _2
- $a represorové proteiny $x chemie $x metabolismus $7 D012097
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a práce podpořená grantem $7 D013485
- 700 1_
- $a Cermáková, Kateřina
- 700 1_
- $a Pachl, Petr
- 700 1_
- $a Sieglová, Irena
- 700 1_
- $a Fábry, Milan
- 700 1_
- $a Otwinowski, Zbyszek
- 700 1_
- $a Rezáčová, Pavlína
- 773 0_
- $w MED00179510 $t Acta crystallographica. Section D, Biological crystallography $x 1399-0047 $g Roč. 68, č. Pt 2 (2012), s. 176-185
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/22281747 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y m $z 0
- 990 __
- $a 20120815 $b ABA008
- 991 __
- $a 20170410103916 $b ABA008
- 999 __
- $a ok $b bmc $g 946234 $s 781414
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2012 $b 68 $c Pt 2 $d 176-185 $e 20120117 $i 1399-0047 $m Acta crystallographica. Section D, Biological crystallography $n Acta Crystallogr D Biol Crystallogr $x MED00179510
- LZP __
- $a Pubmed-20120815/12/02
