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Negative charge of the AC-to-Hly linking segment modulates calcium-dependent membrane activities of Bordetella adenylate cyclase toxin

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F20%3A00531086" target="_blank" >RIV/61388963:_____/20:00531086 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388971:_____/20:00531086 RIV/00216208:11310/20:10414158

  • Result on the web

    <a href="https://www.sciencedirect.com/science/article/pii/S0005273620301413" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0005273620301413</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.bbamem.2020.183310" target="_blank" >10.1016/j.bbamem.2020.183310</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Negative charge of the AC-to-Hly linking segment modulates calcium-dependent membrane activities of Bordetella adenylate cyclase toxin

  • Original language description

    Two distinct conformers of the adenylate cyclase toxin (CyaA) appear to accomplish its two parallel activities within target cell membrane. The translocating conformer would deliver the N-terminal adenylyl cyclase (AC) enzyme domain across plasma membrane into cytosol of cells, while the pore precursor conformer would assemble into oligomeric cation-selective pores and permeabilize cellular membrane. Both toxin activities then involve a membrane-interacting 'AC-to-Hly-linking segment' (residues 400 to 500). Here, we report the NMR structure of the corresponding CyaA(411-490) polypeptide in dodecylphosphocholine micelles and show that it consists of two alpha-helices linked by an unrestrained loop. The N-terminal alpha-helix (Gly418 to His439) remained solvent accessible, while the C-terminal alpha-helix (His457 to Phe485) was fully enclosed within detergent micelles. CyaA(411-490) weakly bound Ca2+ ions (apparent K-D 2.6 mM) and permeabilized negatively charged lipid vesicles. At high concentrations (10 mu M) the CyaA(411-490) polypeptide formed stable conductance units in artificial lipid bilayers with applied voltage, suggesting its possible transmembrane orientation in the membrane-inserted toxin. Mutagenesis revealed that two clusters of negatively charged residues within the 'AC-to-Hly-linking segment' (Glu419 to Glu432 and Asp445 to Glu448) regulate the balance between the AC domain translocating and pore-forming capacities of CyaA in function of calcium concentration.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

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

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2020

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Biochimica Et Biophysica Acta-Biomembranes

  • ISSN

    0005-2736

  • e-ISSN

  • Volume of the periodical

    1862

  • Issue of the periodical within the volume

    9

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    14

  • Pages from-to

    183310

  • UT code for WoS article

    000540854800012

  • EID of the result in the Scopus database

    2-s2.0-85083746018