Molecular basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F17%3A00481651" target="_blank" >RIV/67985823:_____/17:00481651 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/17:10367073 RIV/00216208:11320/17:10367073
Result on the web
<a href="http://dx.doi.org/10.1073/pnas.1714491114" target="_blank" >http://dx.doi.org/10.1073/pnas.1714491114</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1073/pnas.1714491114" target="_blank" >10.1073/pnas.1714491114</a>
Alternative languages
Result language
angličtina
Original language name
Molecular basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1
Original language description
The 14-3-3 proteins, a family of highly conserved scaffolding proteins ubiquitously expressed in all eukaryotic cells, interact with and regulate the function of several hundreds of partner proteins. Yeast neutral trehalases (Nth), enzymes responsible for the hydrolysis of trehalose to glucose, compared with trehalases from other organisms, possess distinct structure and regulation involving phosphorylation at multiple sites followed by binding to the 14-3-3 protein. Here we report the crystal structures of yeast Nth1 and its complex with Bmh1 (yeast 14-3-3 isoform), which, together with mutational and fluorescence studies, indicate that the binding of Nth1 by 14-3-3 triggers Nth1’s activity by enabling the proper 3D configuration of Nth1’s catalytic and calcium-binding domains relative to each other, thus stabilizing the flexible part of the active site required for catalysis. The presented structure of the Bmh1:Nth1 complex highlights the ability of 14-3-3 to modulate the structure of a multidomain binding partner and to function as an allosteric effector. Furthermore, comparison of the Bmh1:Nth1 complex structure with those of 14-3-3:serotonin N-acetyltransferase and 14-3-3:heat shock protein beta-6 complexes revealed similarities in the 3D structures of bound partner proteins, suggesting the highly conserved nature of 14-3-3 affects the structures of many client proteins.
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
10609 - Biochemical research methods
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2017
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Proceedings of the National Academy of Sciences of the United States of America
ISSN
0027-8424
e-ISSN
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Volume of the periodical
114
Issue of the periodical within the volume
46
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
"E9811"-"E9820"
UT code for WoS article
000415173300014
EID of the result in the Scopus database
2-s2.0-85033698958