. . . "7"^^ . "000258595000010" . "DeoR family; CggR; Bacillus subtilis"@en . . "69" . "Krystalov\u00E9 struktury efektor v\u00E1\u017E\u00EDc\u00ED dom\u00E9ny represoru CggR z bakterie Bacillus subtilis ukazuj\u00ED strukturn\u00ED zm\u011Bny po vazb\u011B n\u011Bkolika intermedi\u00E1t\u016F glykol\u00FDzy"@cs . . "Crystal structures of the effector-binding domain of repressor CggR from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates" . . "RIV/68378050:_____/08:00310134" . . "4" . "Crystal structures of the effector-binding domain of repressor CggR from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates" . . . "Joachimiak, A." . "0950-382X" . "1"^^ . "Molecular Microbiology" . "Otwinowski, Z." . "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 . . "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 . . . "GB - Spojen\u00E9 kr\u00E1lovstv\u00ED Velk\u00E9 Brit\u00E1nie a Severn\u00EDho Irska" . "\u0158ez\u00E1\u010Dov\u00E1, Pavl\u00EDna" . "Moy, S. F." . . "Krystalov\u00E9 struktury C-koncov\u00E9 dom\u00E9ny represoru CggR ve voln\u00E9 form\u011B a ve form\u011B v\u00E1zaj\u00EDc\u00ED \u010Dty\u0159i r\u016Fzn\u00E9 ligandy byly ur\u010Deny na rozli\u0161en\u00ED 1.65 a\u017E 1.80 A. Tyto struktury odhaluj\u00ED strukturn\u00ED zm\u011Bny vazebn\u00E9ho m\u00EDsta a dimern\u00EDho rozhran\u00ED spojen\u00E9 se specifickou vazbou ligandu. Vazebn\u00E9 afinity 4 ligand\u016F byly ur\u010Deny isotermalni titra\u010Dn\u00ED kalorimetri\u00ED (ITC). Metodou chemisk\u00E9ho cross-linkingu bylo prok\u00E1z\u00E1no ze oligomerizace CggR je zprost\u0159edkov\u00E1na p\u0159es C-koncovou dom\u00E9nu a zastoupen\u00ED r\u016Fzn\u00FDch oligomer\u016F je ovlivn\u011Bno na p\u0159\u00EDtomnosti ligand\u016F. Test DNA vazebn\u00E9 aktivity prok\u00E1zal destabilizaci CggR/DNA komplexu v p\u0159\u00EDtomnosti fruktozy-1,6-bisfosf\u00E1tu a podobn\u00FD efekt byl pozorov\u00E1n pro dihydroxyacetonfosf\u00E1t. Na\u0161e v\u00FDsledky prokazuj\u00ED, \u017Ee stabilita a funkce CggR je modulov\u00E1na r\u016Fzn\u00FDmi efektory."@cs . . "[EE8D5F5BBA0B]" . "361633" . "Ko\u017E\u00ED\u0161ek, Milan" . "16"^^ . . "Krystalov\u00E9 struktury efektor v\u00E1\u017E\u00EDc\u00ED dom\u00E9ny represoru CggR z bakterie Bacillus subtilis ukazuj\u00ED strukturn\u00ED zm\u011Bny po vazb\u011B n\u011Bkolika intermedi\u00E1t\u016F glykol\u00FDzy"@cs . . "P(1M0508), Z(AV0Z40550506), Z(AV0Z50520514)" . "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 . "RIV/68378050:_____/08:00310134!RIV09-AV0-68378050" . . "Machius, M." . "Sieglov\u00E1, Irena" . . "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." .