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1.2 °A resolution crystal structure of Escherichia coli WrbA holoprotein

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F13%3A00399208" target="_blank" >RIV/61388971:_____/13:00399208 - isvavai.cz</a>

  • Alternative codes found

    RIV/67179843:_____/13:00399208 RIV/68378050:_____/13:00399208

  • Result on the web

    <a href="http://dx.doi.org/10.1107/S0907444913017162" target="_blank" >http://dx.doi.org/10.1107/S0907444913017162</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1107/S0907444913017162" target="_blank" >10.1107/S0907444913017162</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    1.2 °A resolution crystal structure of Escherichia coli WrbA holoprotein

  • Original language description

    The Escherichia coli protein WrbA, an FMN-dependent NAD(P)H:quinone oxidoreductase, was crystallized under new conditions in the presence of FAD or the native cofactor FMN. Slow-growing deep yellow crystals formed with FAD display the tetragonal bipyramidal shape typical for WrbA and diffract to 1.2?? resolution, the highest yet reported. Faster-growing deep yellow crystals formed with FMN display an atypical shape, but diffract to only 1.6?? resolution and are not analysed further here. The 1.2?? resolution structure detailed here revealed only FMN in the active site and no electron density that can accommodate the missing parts of FAD. The very high resolution supports the modelling of the FMN isoalloxazine with a small but distinct propeller twist,apparently the first experimental observation of this predicted conformation, which appears to be enforced by the protein through a network of hydrogen bonds. Comparison of the electron density of the twisted isoalloxazine ring with the r

  • 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

    <a href="/en/project/GAP207%2F10%2F1934" target="_blank" >GAP207/10/1934: Structural insight into E. coli protein WrbA, the founding member of a family of proteins implicated in defense of cells against oxidative stress</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2013

  • 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-Biological Crystallography

  • ISSN

    0907-4449

  • e-ISSN

  • Volume of the periodical

    69

  • Issue of the periodical within the volume

    9

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    10

  • Pages from-to

    1748-1757

  • UT code for WoS article

    000324818000012

  • EID of the result in the Scopus database