| Attributes | Values |
|---|
| rdf:type
| |
| Description
| - Krystalové struktury C-koncové domény represoru CggR ve volné formě a ve formě vázající čtyři různé ligandy byly určeny na rozlišení 1.65 až 1.80 A. Tyto struktury odhalují strukturní změny vazebného místa a dimerního rozhraní spojené se specifickou vazbou ligandu. Vazebné afinity 4 ligandů byly určeny isotermalni titrační kalorimetrií (ITC). Metodou chemiského cross-linkingu bylo prokázáno ze oligomerizace CggR je zprostředkována přes C-koncovou doménu a zastoupení různých oligomerů je ovlivněno na přítomnosti ligandů. Test DNA vazebné aktivity prokázal destabilizaci CggR/DNA komplexu v přítomnosti fruktozy-1,6-bisfosfátu a podobný efekt byl pozorován pro dihydroxyacetonfosfát. Naše výsledky prokazují, že stabilita a funkce CggR je modulována různými efektory. (cs)
- Crystal structures of the C-terminal effector-binding domain of CggR, both unliganded as well as in complex with the four ligands at resolutions between 1.65 and 1.80 A reveal unique ligand-specific structural changes in the binding site that affect the dimer interface. Binding affinities of these ligands were determined by isothermal titration calorimetry. Chemical cross-linking shows that CggR oligomerization is mediated through its effector-binding domain, and that binding of the different ligands differentially affects the distribution of oligomers. Electrophoretic mobility shift assays (EMSAs) confirmed a destabilizing effect of fructose-1,6-bisphosphate on the CggR/ DNA complex, and also showed similar effects for dihydroxyacetone phosphate. Our results suggest that CggR stability and function may be modulated by various effectors in a complex fashion.
- Crystal structures of the C-terminal effector-binding domain of CggR, both unliganded as well as in complex with the four ligands at resolutions between 1.65 and 1.80 A reveal unique ligand-specific structural changes in the binding site that affect the dimer interface. Binding affinities of these ligands were determined by isothermal titration calorimetry. Chemical cross-linking shows that CggR oligomerization is mediated through its effector-binding domain, and that binding of the different ligands differentially affects the distribution of oligomers. Electrophoretic mobility shift assays (EMSAs) confirmed a destabilizing effect of fructose-1,6-bisphosphate on the CggR/ DNA complex, and also showed similar effects for dihydroxyacetone phosphate. Our results suggest that CggR stability and function may be modulated by various effectors in a complex fashion. (en)
|
| Title
| - Crystal structures of the effector-binding domain of repressor CggR from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates
- Crystal structures of the effector-binding domain of repressor CggR from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates (en)
- Krystalové struktury efektor vážící domény represoru CggR z bakterie Bacillus subtilis ukazují strukturní změny po vazbě několika intermediátů glykolýzy (cs)
|
| skos:prefLabel
| - Crystal structures of the effector-binding domain of repressor CggR from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates
- Crystal structures of the effector-binding domain of repressor CggR from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates (en)
- Krystalové struktury efektor vážící domény represoru CggR z bakterie Bacillus subtilis ukazují strukturní změny po vazbě několika intermediátů glykolýzy (cs)
|
| skos:notation
| - RIV/68378050:_____/08:00310134!RIV09-AV0-68378050
|
| http://linked.open...avai/riv/aktivita
| |
| http://linked.open...avai/riv/aktivity
| - P(1M0508), Z(AV0Z40550506), Z(AV0Z50520514)
|
| http://linked.open...iv/cisloPeriodika
| |
| http://linked.open...vai/riv/dodaniDat
| |
| http://linked.open...aciTvurceVysledku
| |
| http://linked.open.../riv/druhVysledku
| |
| http://linked.open...iv/duvernostUdaju
| |
| http://linked.open...titaPredkladatele
| |
| http://linked.open...dnocenehoVysledku
| |
| http://linked.open...ai/riv/idVysledku
| - RIV/68378050:_____/08:00310134
|
| http://linked.open...riv/jazykVysledku
| |
| http://linked.open.../riv/klicovaSlova
| - DeoR family; CggR; Bacillus subtilis (en)
|
| http://linked.open.../riv/klicoveSlovo
| |
| http://linked.open...odStatuVydavatele
| - GB - Spojené království Velké Británie a Severního Irska
|
| http://linked.open...ontrolniKodProRIV
| |
| http://linked.open...i/riv/nazevZdroje
| |
| http://linked.open...in/vavai/riv/obor
| |
| http://linked.open...ichTvurcuVysledku
| |
| http://linked.open...cetTvurcuVysledku
| |
| http://linked.open...vavai/riv/projekt
| |
| http://linked.open...UplatneniVysledku
| |
| http://linked.open...v/svazekPeriodika
| |
| http://linked.open...iv/tvurceVysledku
| - Kožíšek, Milan
- Sieglová, Irena
- Řezáčová, Pavlína
- Otwinowski, Z.
- Joachimiak, A.
- Machius, M.
- Moy, S. F.
|
| http://linked.open...ain/vavai/riv/wos
| |
| http://linked.open...n/vavai/riv/zamer
| |
| issn
| |
| number of pages
| |
![[RDF Data]](/fct/images/sw-rdf-blue.png)
![[cxml]](/fct/images/cxml_doc.png)
![[csv]](/fct/images/csv_doc.png)
![[text]](/fct/images/ntriples_doc.png)
![[turtle]](/fct/images/n3turtle_doc.png)
![[ld+json]](/fct/images/jsonld_doc.png)
![[rdf+json]](/fct/images/json_doc.png)
![[rdf+xml]](/fct/images/xml_doc.png)
![[atom+xml]](/fct/images/atom_doc.png)
![[html]](/fct/images/html_doc.png)