ATP and Magnesium Drive Conformational Changes of the Na+/K+-ATPase Cytoplasmic Headpiece
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F09%3A00010133" target="_blank" >RIV/61989592:15310/09:00010133 - isvavai.cz</a>
Alternative codes found
RIV/67985823:_____/09:00327403 RIV/00216208:11130/09:5288
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
ATP and Magnesium Drive Conformational Changes of the Na+/K+-ATPase Cytoplasmic Headpiece
Original language description
Conformational changes of the Na+/K+-ATPase isolated large cytoplasmic segment connecting transmembrane helices M4 and M5 (C45) induced by the interaction with enzyme ligands (i.e. Mg2+ and/or ATP) were investigated by means of the intrinsic tryptophan fluorescence measurement and molecular dynamic simulations. Our data revealed that this model system consisting of only two domains retained the ability to adopt open or closed conformation, i.e. behavior, which is expected from the crystal structures ofrelative Ca2+-ATPase from sarco(endo)plasmic reticulum for the corresponding part of the entire enzyme. Our data revealed that the C45 is found in the closed conformation in the absence of any ligand, in the presence of Mg2+ only, or in the simultaneouspresence of Mg2+ and ATP. Binding of the ATP alone (i.e. in the absence of Mg2+) induced open conformation of the C45. The fact that the transmembrane part of the enzyme was absent in our experiments suggested that the observed conformati
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach
Others
Publication year
2009
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biochimica et Biophysica Acta - Biomembranes
ISSN
0005-2736
e-ISSN
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Volume of the periodical
1788
Issue of the periodical within the volume
5
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
11
Pages from-to
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UT code for WoS article
000266190600019
EID of the result in the Scopus database
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