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
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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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