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Structural insight into DNA recognition by bacterial transcriptional regulators of the SorC/DeoR family

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F21%3A00548688" target="_blank" >RIV/61388963:_____/21:00548688 - isvavai.cz</a>

  • Alternative codes found

    RIV/68378050:_____/21:00548549

  • Result on the web

    <a href="https://doi.org/10.1107/S2059798321009633" target="_blank" >https://doi.org/10.1107/S2059798321009633</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1107/S2059798321009633" target="_blank" >10.1107/S2059798321009633</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Structural insight into DNA recognition by bacterial transcriptional regulators of the SorC/DeoR family

  • Original language description

    The SorC/DeoR family is a large family of bacterial transcription regulators that are involved in the control of carbohydrate metabolism and quorum sensing. To understand the structural basis of DNA recognition, structural studies of two functionally characterized SorC/DeoR family members from Bacillus subtilis were performed: the deoxyribonucleoside regulator bsDeoR and the central glycolytic genes regulator bsCggR. Each selected protein represents one of the subgroups that are recognized within the family. Crystal structures were determined of the N-terminal DNA-binding domains of bsDeoR and bsCggR in complex with DNA duplexes representing the minimal operator sequence at resolutions of 2.3 and 2.1 Å, respectively. While bsDeoRDBD contains a homeodomain-like HTH-type domain, bsCggRDBD contains a winged helix–turn–helix-type motif. Both proteins form C2-symmetric dimers that recognize two consecutive major grooves, and the protein–DNA interactions have been analyzed in detail. The crystal structures were used to model the interactions of the proteins with the full DNA operators, and a common mode of DNA recognition is proposed that is most likely to be shared by other members of the SorC/DeoR family.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    <a href="/en/project/EF16_019%2F0000729" target="_blank" >EF16_019/0000729: Chemical biology for drugging undruggable targets</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2021

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Acta Crystallographica Section D-Structural Biology

  • ISSN

    2059-7983

  • e-ISSN

    2059-7983

  • Volume of the periodical

    77

  • Issue of the periodical within the volume

    11

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    14

  • Pages from-to

    1411-1424

  • UT code for WoS article

    000714429000008

  • EID of the result in the Scopus database

    2-s2.0-85118954561