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Significant changes between the X-ray structure and NMR structure of delta subunit of RNA polymerase

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F12%3A00057460" target="_blank" >RIV/00216224:14740/12:00057460 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    čeština

  • Original language name

    Significant changes between the Xray structure and NMR structure of delta subunit of RNA polymerase

  • Original language description

    RNA polymerase is an essential enzyme. RNAP from gram negative bacteria contain two additional subunits. The delta subunit is 173 aminoacids long and comes from Bacillus subtilis. The N terminal domain displays an ordered structure and the C terminal domain appears to be flexible and unstructured. The N terminal domain was solved either with NMR and Xray. The Xray structure showed completely different behaviour in the region corresponding to beta sheets present in NMR structure. In the Xray structure were found nickel ions which may have a significant effect on the folding of the protein. This is a strong proof that some of the proteins can be differently structured in the solution as in the crystalline phase.

  • Czech name

    Significant changes between the Xray structure and NMR structure of delta subunit of RNA polymerase

  • Czech description

    RNA polymerase is an essential enzyme. RNAP from gram negative bacteria contain two additional subunits. The delta subunit is 173 aminoacids long and comes from Bacillus subtilis. The N terminal domain displays an ordered structure and the C terminal domain appears to be flexible and unstructured. The N terminal domain was solved either with NMR and Xray. The Xray structure showed completely different behaviour in the region corresponding to beta sheets present in NMR structure. In the Xray structure were found nickel ions which may have a significant effect on the folding of the protein. This is a strong proof that some of the proteins can be differently structured in the solution as in the crystalline phase.

Classification

  • Type

    O - Miscellaneous

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GD301%2F09%2FH004" target="_blank" >GD301/09/H004: Molecular and structural biology of selected antitumor drugs. From mechanistic studies to chemotherapy of tumors</a><br>

  • Continuities

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

Others

  • Publication year

    2012

  • Confidentiality

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