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Structural basis for long-chain isoprenoid synthesis by cis-prenyltransferases

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F22%3A00557998" target="_blank" >RIV/61388971:_____/22:00557998 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216224:14740/22:00128766

  • Result on the web

    <a href="https://www.science.org/doi/10.1126/sciadv.abn1171" target="_blank" >https://www.science.org/doi/10.1126/sciadv.abn1171</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1126/sciadv.abn1171" target="_blank" >10.1126/sciadv.abn1171</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Structural basis for long-chain isoprenoid synthesis by cis-prenyltransferases

  • Original language description

    Isoprenoids are synthesized by the prenyltransferase superfamily, which is subdivided according to the product stereoisomerism and length. In short- and medium-chain isoprenoids, product length correlates with active site volume. However, enzymes synthesizing long-chain products and rubber synthases fail to conform to this paradigm, because of an unexpectedly small active site. Here, we focused on the human cis-prenyltransferase complex (hcis-PT), residing at the endoplasmic reticulum membrane and playing a crucial role in protein glycosylation. Crystallographic investigation of hcis-PT along the reaction cycle revealed an outlet for the elongating product. Hydrogen-deuterium exchange mass spectrometry analysis showed that the hydrophobic active site core is flanked by dynamic regions consistent with separate inlet and outlet orifices. Last, using a fluorescence substrate analog, we show that product elongation and membrane association are closely correlated. Together, our results support direct membrane insertion of the elongating isoprenoid during catalysis, uncoupling active site volume from product length.

  • 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

    <a href="/en/project/ED1.1.00%2F02.0109" target="_blank" >ED1.1.00/02.0109: Biotechnology and Biomedicine Centre of the Academy of Sciences and Charles University</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2022

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Science Advances

  • ISSN

    2375-2548

  • e-ISSN

    2375-2548

  • Volume of the periodical

    8

  • Issue of the periodical within the volume

    20

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    14

  • Pages from-to

    eabn1171

  • UT code for WoS article

    000798164800022

  • EID of the result in the Scopus database

    2-s2.0-85130283475