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Protonation states of the key active site residues and structural dynamics of the glmS riboswitch as revealed by molecular dynamics

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F10%3A00347709" target="_blank" >RIV/68081707:_____/10:00347709 - isvavai.cz</a>

  • Alternative codes found

    RIV/68081707:_____/10:00373421

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Protonation states of the key active site residues and structural dynamics of the glmS riboswitch as revealed by molecular dynamics

  • Original language description

    The glmS catalytic riboswitch is part of the 5?-untranslated region of mRNAs encoding glucosamine-6-phosphate (GlcN6P) synthetase (glmS) in numerous Gram-positive bacteria. Binding of the cofactor GlcN6P induces site-specific self-cleavage of the RNA. However, detailed reaction mechanism as well as protonation state of glmS reactive form remains still elusive. To probe the dominant protonation states of key active site residues, we carried out explicit solvent molecular dynamic simulations involving various protonation states of three crucial active site moieties observed in the available crystal structures: (i) guanine G40 (following the T. tengcongensis numbering), (ii) the GlcN6P amino/ammonium group, and (iii) the GlcN6P phosphate moiety.

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    BO - Biophysics

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2010

  • 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 Physical Chemistry B

  • ISSN

    1520-6106

  • e-ISSN

  • Volume of the periodical

    114

  • Issue of the periodical within the volume

    26

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    12

  • Pages from-to

  • UT code for WoS article

    000279282600015

  • EID of the result in the Scopus database