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Phosphate binding in the active centre of tomato multifunctional nuclease TBN1 and analysis of superhelix formation by the enzyme

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F15%3A43899762" target="_blank" >RIV/60461373:22330/15:43899762 - isvavai.cz</a>

  • Result on the web

    <a href="http://scripts.iucr.org/cgi-bin/paper?S2053230X15018324" target="_blank" >http://scripts.iucr.org/cgi-bin/paper?S2053230X15018324</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1107/S2053230X15018324" target="_blank" >10.1107/S2053230X15018324</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Phosphate binding in the active centre of tomato multifunctional nuclease TBN1 and analysis of superhelix formation by the enzyme

  • Original language description

    Tomato multifunctional nuclease TBN1 belongs to the type I nuclease family, which plays an important role in apoptotic processes and cell senescence in plants. The newly solved structure of the N211D mutant is reported. Although the main crystal-packingmotif (the formation of superhelices) is conserved, the details differ among the known structures. A phosphate ion was localized in the active site of the enzyme. The binding of the surface loop to the active centre is stabilized by the phosphate ion, which correlates with the observed aggregation of TBN1 in phosphate buffer. The conserved binding of the surface loop to the active centre suggests biological relevance of the contact in a regulatory function or in the formation of oligomers.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2015

  • 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 F-Structural Biology and Crystallization Communications

  • ISSN

    1744-3091

  • e-ISSN

  • Volume of the periodical

    71

  • Issue of the periodical within the volume

    1.11.2015

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    8

  • Pages from-to

    1408-1415

  • UT code for WoS article

    000364557700008

  • EID of the result in the Scopus database