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Calcium-Driven Folding of RTX Domain b-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F16%3A10326639" target="_blank" >RIV/00216208:11310/16:10326639 - isvavai.cz</a>

  • Result on the web

    <a href="http://www.sciencedirect.com/science/article/pii/S1097276516300016" target="_blank" >http://www.sciencedirect.com/science/article/pii/S1097276516300016</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.molcel.2016.03.018" target="_blank" >10.1016/j.molcel.2016.03.018</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Calcium-Driven Folding of RTX Domain b-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts

  • Original language description

    Calcium-binding RTX proteins are equipped with C-terminal secretion signals and translocate from the Ca(2+)-depleted cytosol of Gram-negative bacteria directly into the Ca(2+)-rich external milieu, passing through the "channel-tunnel" ducts of type I secretion systems (T1SSs). Using Bordetella pertussis adenylate cyclase toxin, we solved the structure of an essential C-terminal assembly that caps the RTX domains of RTX family leukotoxins. This is shown to scaffold directional Ca(2+)-dependent folding of the carboxy-proximal RTX repeat blocks into β-rolls. The resulting intramolecular Brownian ratchets then prevent backsliding of translocating RTX proteins in the T1SS conduits and thereby accelerate excretion of very large RTX leukotoxins from bacterial cells by a vectorial "push-ratchet" mechanism. Successive Ca(2+)-dependent and cosecretional acquisition of a functional RTX toxin structure in the course of T1SS-mediated translocation, through RTX domain folding from the C-terminal cap toward the N terminus, sets a paradigm that opens for design of virulence inhibitors of major pathogens.

  • 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

    S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2016

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Molecular Cell

  • ISSN

    1097-2765

  • e-ISSN

  • Volume of the periodical

    62

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    17

  • Pages from-to

    46-62

  • UT code for WoS article

    000374119600007

  • EID of the result in the Scopus database

    2-s2.0-84962446659