-
Je něco špatně v tomto záznamu ?
Molecular basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1
M. Alblova, A. Smidova, V. Docekal, J. Vesely, P. Herman, V. Obsilova, T. Obsil,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Free Medical Journals
od 1915 do Před 6 měsíci
Freely Accessible Science Journals
od 1915 do Před 6 měsíci
PubMed Central
od 1915 do Před 6 měsíci
Europe PubMed Central
od 1915 do Před 6 měsíci
Open Access Digital Library
od 1915-01-15
Open Access Digital Library
od 1915-01-01
PubMed
29087344
DOI
10.1073/pnas.1714491114
Knihovny.cz E-zdroje
- MeSH
- arylalkylamin-N-acetyltransferasa metabolismus MeSH
- chemické databáze * MeSH
- fosforylace MeSH
- glukosa metabolismus MeSH
- katalytická doména MeSH
- konformace proteinů MeSH
- krystalografie rentgenová MeSH
- molekulární modely MeSH
- proteinové domény MeSH
- proteiny 14-3-3 genetika metabolismus MeSH
- proteiny teplotního šoku chemie metabolismus MeSH
- Saccharomyces cerevisiae - proteiny chemie metabolismus MeSH
- Saccharomyces cerevisiae enzymologie genetika metabolismus MeSH
- trehalasa chemie metabolismus MeSH
- trehalosa metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
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.
Citace poskytuje Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc18024518
- 003
- CZ-PrNML
- 005
- 20180710092723.0
- 007
- ta
- 008
- 180709s2017 xxu f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1073/pnas.1714491114 $2 doi
- 035 __
- $a (PubMed)29087344
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a xxu
- 100 1_
- $a Alblova, Miroslava $u Department of Structural Biology of Signaling Proteins, Division Biotechnology and Biomedicine Center of the Academy of Sciences and Charles University in Vestec (BIOCEV), Institute of Physiology, The Czech Academy of Sciences, Prague 14220, Czech Republic.
- 245 10
- $a Molecular basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1 / $c M. Alblova, A. Smidova, V. Docekal, J. Vesely, P. Herman, V. Obsilova, T. Obsil,
- 520 9_
- $a 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.
- 650 _2
- $a proteiny 14-3-3 $x genetika $x metabolismus $7 D048948
- 650 _2
- $a arylalkylamin-N-acetyltransferasa $x metabolismus $7 D047068
- 650 _2
- $a katalytická doména $7 D020134
- 650 _2
- $a krystalografie rentgenová $7 D018360
- 650 12
- $a chemické databáze $7 D062126
- 650 _2
- $a glukosa $x metabolismus $7 D005947
- 650 _2
- $a proteiny teplotního šoku $x chemie $x metabolismus $7 D006360
- 650 _2
- $a molekulární modely $7 D008958
- 650 _2
- $a fosforylace $7 D010766
- 650 _2
- $a konformace proteinů $7 D011487
- 650 _2
- $a proteinové domény $7 D000072417
- 650 _2
- $a Saccharomyces cerevisiae $x enzymologie $x genetika $x metabolismus $7 D012441
- 650 _2
- $a Saccharomyces cerevisiae - proteiny $x chemie $x metabolismus $7 D029701
- 650 _2
- $a trehalasa $x chemie $x metabolismus $7 D014198
- 650 _2
- $a trehalosa $x metabolismus $7 D014199
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a práce podpořená grantem $7 D013485
- 700 1_
- $a Smidova, Aneta $u Department of Structural Biology of Signaling Proteins, Division Biotechnology and Biomedicine Center of the Academy of Sciences and Charles University in Vestec (BIOCEV), Institute of Physiology, The Czech Academy of Sciences, Prague 14220, Czech Republic. Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, Prague 12843, Czech Republic.
- 700 1_
- $a Docekal, Vojtech $u Department of Organic Chemistry, Faculty of Science, Charles University, Prague 12843, Czech Republic.
- 700 1_
- $a Vesely, Jan $u Department of Organic Chemistry, Faculty of Science, Charles University, Prague 12843, Czech Republic.
- 700 1_
- $a Herman, Petr $u Institute of Physics, Faculty of Mathematics and Physics, Charles University, Prague 12116, Czech Republic.
- 700 1_
- $a Obsilova, Veronika $u Department of Structural Biology of Signaling Proteins, Division Biotechnology and Biomedicine Center of the Academy of Sciences and Charles University in Vestec (BIOCEV), Institute of Physiology, The Czech Academy of Sciences, Prague 14220, Czech Republic; veronika.obsilova@fgu.cas.cz obsil@natur.cuni.cz.
- 700 1_
- $a Obsil, Tomas $u Department of Structural Biology of Signaling Proteins, Division Biotechnology and Biomedicine Center of the Academy of Sciences and Charles University in Vestec (BIOCEV), Institute of Physiology, The Czech Academy of Sciences, Prague 14220, Czech Republic; veronika.obsilova@fgu.cas.cz obsil@natur.cuni.cz. Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, Prague 12843, Czech Republic.
- 773 0_
- $w MED00010472 $t Proceedings of the National Academy of Sciences of the United States of America $x 1091-6490 $g Roč. 114, č. 46 (2017), s. E9811-E9820
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/29087344 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y a $z 0
- 990 __
- $a 20180709 $b ABA008
- 991 __
- $a 20180710093013 $b ABA008
- 999 __
- $a ok $b bmc $g 1316649 $s 1021439
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2017 $b 114 $c 46 $d E9811-E9820 $e 20171030 $i 1091-6490 $m Proceedings of the National Academy of Sciences of the United States of America $n Proc Natl Acad Sci U S A $x MED00010472
- LZP __
- $a Pubmed-20180709
