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Substrate binding activates the designed triple mutant of the colicin E7 metallonuclease

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F14%3A00436908" target="_blank" >RIV/61388963:_____/14:00436908 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1007/s00775-014-1186-6" target="_blank" >http://dx.doi.org/10.1007/s00775-014-1186-6</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/s00775-014-1186-6" target="_blank" >10.1007/s00775-014-1186-6</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Substrate binding activates the designed triple mutant of the colicin E7 metallonuclease

  • Original language description

    The nuclease domain of colicin E7 (NColE7) cleaves DNA nonspecifically. The active center is a Zn2+-containing HNH motif at the C-terminus. The N-terminal loop is essential for the catalytic activity providing opportunity for allosteric modulation of theenzyme. To identify the key residues responsible for the structural integrity of NColE7, a virtual alanine scan was performed on a semiempirical quantum chemical level within the 25 residue long N-terminal sequence (446-470). Based on the calculations the T454A/K458A/W464A-NColE7 triple mutant (TKW) was expressed and purified. According to the agarose gel electrophoresis experiments and linear dichroism spectra the catalytic activity of the TKW mutant decreased in comparison with wild-type NColE7. Thedistorted structure and weakened Zn2+ binding may account for this as revealed by circular dichroism spectra, mass spectrometry, fluorescence-based thermal analysis and isothermal microcalorimetric titrations. Remarkably, the substrate in

  • 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

    2014

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of Biological Inorganic Chemistry

  • ISSN

    0949-8257

  • e-ISSN

  • Volume of the periodical

    19

  • Issue of the periodical within the volume

    8

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    9

  • Pages from-to

    1295-1303

  • UT code for WoS article

    000345403900005

  • EID of the result in the Scopus database