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

Result code in 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>

Alternative codes found

RIV/68378050:_____/14:00434086

Result on the web

<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>

Result language

angličtina

Original language name

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

Original language description

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

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

<a href="/en/project/ME08016" target="_blank" >ME08016: Structural studies of transcriptional regulators of the DeoR and GntR families involved in catabolic repression in Bacillus subtilis.</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2014

Confidentiality

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

Name of the periodical

FEBS Journal

ISSN

1742-464X

e-ISSN

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Volume of the periodical

281

Issue of the periodical within the volume

18

Country of publishing house

GB - UNITED KINGDOM

Number of pages

13

Pages from-to

4280-4292

UT code for WoS article

000342584200023

EID of the result in the Scopus database

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