A refined atomic scale model of the Saccharomyces cerevisiae K+-translocation protein Trk1p combined with experimental evidence confirms the role of selectivity filter glycines and other key residues
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F15%3A43888965" target="_blank" >RIV/60076658:12310/15:43888965 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/86652079:_____/15:00473351
Výsledek na webu
<a href="http://www.sciencedirect.com/science/article/pii/S0005273615000474" target="_blank" >http://www.sciencedirect.com/science/article/pii/S0005273615000474</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bbamem.2015.02.007" target="_blank" >10.1016/j.bbamem.2015.02.007</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
A refined atomic scale model of the Saccharomyces cerevisiae K+-translocation protein Trk1p combined with experimental evidence confirms the role of selectivity filter glycines and other key residues
Popis výsledku v původním jazyce
Potassium ion (K+) uptake in yeast is mediated mainly by the Trk1/2 proteins that enable cells to survive on external K+ concentration as low as a few mu M. Fungal Trks are related to prokaryotic TRK and Ktr and plant HKT K+ transport systems. Overall sequence similarity is very low, thus requiring experimental verification of homology models. Here a refined structural model of the Saccharomyces cerevisiae Trk1 is presented that was obtained by combining homology modeling, molecular dynamics simulationand experimental verification through functional analysis of mutants. Structural models and experimental results showed that glycines within the selectivity filter, conserved among the K-channel/transporter family, are not only important for protein function, but are also required for correct folding/membrane targeting. A conserved aspartic acid in the P-A helix (D79) and a lysine in the M2(D) helix (K1147) were proposed earlier to interact. Our results suggested individual roles of thes
Název v anglickém jazyce
A refined atomic scale model of the Saccharomyces cerevisiae K+-translocation protein Trk1p combined with experimental evidence confirms the role of selectivity filter glycines and other key residues
Popis výsledku anglicky
Potassium ion (K+) uptake in yeast is mediated mainly by the Trk1/2 proteins that enable cells to survive on external K+ concentration as low as a few mu M. Fungal Trks are related to prokaryotic TRK and Ktr and plant HKT K+ transport systems. Overall sequence similarity is very low, thus requiring experimental verification of homology models. Here a refined structural model of the Saccharomyces cerevisiae Trk1 is presented that was obtained by combining homology modeling, molecular dynamics simulationand experimental verification through functional analysis of mutants. Structural models and experimental results showed that glycines within the selectivity filter, conserved among the K-channel/transporter family, are not only important for protein function, but are also required for correct folding/membrane targeting. A conserved aspartic acid in the P-A helix (D79) and a lysine in the M2(D) helix (K1147) were proposed earlier to interact. Our results suggested individual roles of thes
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CE - Biochemie
OECD FORD obor
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Návaznosti výsledku
Projekt
<a href="/cs/project/GA13-21053S" target="_blank" >GA13-21053S: Studium symetrického alosterického mechanismu hexamerického argininového represoru z E.coli pomoci počitačových simulací</a><br>
Návaznosti
S - Specificky vyzkum na vysokych skolach
Ostatní
Rok uplatnění
2015
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Biochimica et Biophysica Acta- Biomembranes
ISSN
0005-2736
e-ISSN
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Svazek periodika
1848
Číslo periodika v rámci svazku
5
Stát vydavatele periodika
NL - Nizozemsko
Počet stran výsledku
13
Strana od-do
1183-1195
Kód UT WoS článku
000352041100013
EID výsledku v databázi Scopus
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