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Phage tail fibre assembly proteins employ a modular structure to drive the correct folding of diverse fibres

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F19%3A00113245" target="_blank" >RIV/00216224:14740/19:00113245 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1038/s41564-019-0477-7" target="_blank" >http://dx.doi.org/10.1038/s41564-019-0477-7</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1038/s41564-019-0477-7" target="_blank" >10.1038/s41564-019-0477-7</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Phage tail fibre assembly proteins employ a modular structure to drive the correct folding of diverse fibres

  • Original language description

    Phage tail fibres are elongated protein assemblies capable of specific recognition of bacterial surfaces during the first step of viral infection(1-4). The folding of these complex trimeric structures often requires a phage-encoded tail fibre assembly (Tfa) proteins(5-7). Despite the wide occurrence of Tfa proteins, their functional mechanism has not been elucidated. Here, we investigate the tail fibre and Tfa of Escherichia coli phage Mu. We demonstrate that Tfa forms a stable complex with the tail fibre, and present a 2.1 angstrom resolution X-ray crystal structure of this complex. We find that Tfa proteins are comprised of two domains: a non-conserved N-terminal domain that binds to the C-terminal region of the fibre and a conserved C-terminal domain that probably mediates fibre oligomerization and assembly. Tfa forms rapidly exchanging multimers on its own, but not a stable trimer, implying that Tfa does not specify the trimeric state of the fibre. We propose that the key conserved role of Tfa is to ensure that fibre assembly and multimerization initiates at the C terminus, ensuring that the intertwined and repetitive structural elements of fibres come together in the correct sequence. The universal importance of correctly aligning the C termini of phage fibres is highlighted by our work.

  • 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

    10606 - Microbiology

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2019

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Nature Microbiology

  • ISSN

    2058-5276

  • e-ISSN

  • Volume of the periodical

    4

  • Issue of the periodical within the volume

    10

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    9

  • Pages from-to

    1645-1653

  • UT code for WoS article

    000487286800010

  • EID of the result in the Scopus database

    2-s2.0-85068091527