Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F14%3A00434086" target="_blank" >RIV/61388963:_____/14:00434086 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/68378050:_____/14:00434086

Výsledek na webu

<a href="http://dx.doi.org/10.1111/febs.12856" target="_blank" >http://dx.doi.org/10.1111/febs.12856</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1111/febs.12856" target="_blank" >10.1111/febs.12856</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis

Popis výsledku v původním jazyce

Deoxyribonucleoside regulator (DeoR) from Bacillus subtilis negatively regulates expression of enzymes involved in the catabolism of deoxyribonucleosides and deoxyribose. The DeoR protein is homologous to the sorbitol operon regulator family of metabolicregulators and comprises an N-terminal DNA-binding domain and a C-terminal effector-binding domain. We have determined the crystal structure of the effector-binding domain of DeoR (C-DeoR) in free form and in covalent complex with its effector deoxyribose-5-phosphate (dR5P). This is the first case of a covalently attached effector molecule captured in the structure of a bacterial transcriptional regulator. The dR5P molecule is attached through a Schiff base linkage to residue Lys141. The crucial role of Lys141 in effector binding was confirmed by mutational analysis and mass spectrometry of Schiff base adducts formed in solution. Structural analyses of the free and effector-bound C-DeoR structures provided a structural explanation for

Název v anglickém jazyce

Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis

Popis výsledku anglicky

Deoxyribonucleoside regulator (DeoR) from Bacillus subtilis negatively regulates expression of enzymes involved in the catabolism of deoxyribonucleosides and deoxyribose. The DeoR protein is homologous to the sorbitol operon regulator family of metabolicregulators and comprises an N-terminal DNA-binding domain and a C-terminal effector-binding domain. We have determined the crystal structure of the effector-binding domain of DeoR (C-DeoR) in free form and in covalent complex with its effector deoxyribose-5-phosphate (dR5P). This is the first case of a covalently attached effector molecule captured in the structure of a bacterial transcriptional regulator. The dR5P molecule is attached through a Schiff base linkage to residue Lys141. The crucial role of Lys141 in effector binding was confirmed by mutational analysis and mass spectrometry of Schiff base adducts formed in solution. Structural analyses of the free and effector-bound C-DeoR structures provided a structural explanation for

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/ME08016" target="_blank" >ME08016: Strukturní studie transkripčních regulátorů rodiny DeoR a GntR účastnících se katabolické represe v bakterii Bacillus subtilis.</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

FEBS Journal

ISSN

1742-464X

e-ISSN

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Svazek periodika

281

Číslo periodika v rámci svazku

18

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

13

Strana od-do

4280-4292

Kód UT WoS článku

000342584200023

EID výsledku v databázi Scopus

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