About: ATP and Magnesium Drive Conformational Changes of the Na+/K+-ATPase Cytoplasmic Headpiece

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: ATP and Magnesium Drive Conformational Changes of the Na+/K+-ATPase Cytoplasmic Headpiece Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
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 of relative 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 simultaneous presence 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 conformational changes are 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 of relative 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 simultaneous presence 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 conformational changes are (en)
Title	ATP and Magnesium Drive Conformational Changes of the Na+/K+-ATPase Cytoplasmic Headpiece ATP and Magnesium Drive Conformational Changes of the Na+/K+-ATPase Cytoplasmic Headpiece (en)
skos:prefLabel	ATP and Magnesium Drive Conformational Changes of the Na+/K+-ATPase Cytoplasmic Headpiece ATP and Magnesium Drive Conformational Changes of the Na+/K+-ATPase Cytoplasmic Headpiece (en)
skos:notation	RIV/61989592:15310/09:00010133!RIV10-MSM-15310___
http://linked.open...avai/riv/aktivita	P S Z
http://linked.open...avai/riv/aktivity	P(GA203/07/0564), P(GA303/07/0915), P(GD522/08/H003), P(LC512), S, Z(AV0Z50110509), Z(MSM6198959215), Z(MSM6198959216)
http://linked.open...iv/cisloPeriodika	5
http://linked.open...vai/riv/dodaniDat	2010
http://linked.open...aciTvurceVysledku	Kubala, Martin Janovská, Marika Otyepka, Michal Sklenovský, Petr
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Palackého v Olomouci / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	304350
http://linked.open...ai/riv/idVysledku	RIV/61989592:15310/09:00010133
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Na+/K+-ATPase; P-type ATPase; ATP; magnesium; tryptophan fluorescence; conformational change (en)
http://linked.open.../riv/klicoveSlovo	ATP conformational change P-type ATPase tryptophan fluorescence magnesium Na+/K+-ATPase
http://linked.open...odStatuVydavatele	NL - Nizozemsko
http://linked.open...ontrolniKodProRIV	[D84C903E6381]
http://linked.open...i/riv/nazevZdroje	Biochimica et Biophysica Acta - Biomembranes
http://linked.open...in/vavai/riv/obor	BO
http://linked.open...ichTvurcuVysledku	4 (xsd:int)
http://linked.open...cetTvurcuVysledku	8 (xsd:int)
http://linked.open...vavai/riv/projekt	Center for biomolecules and complex molecular systems Integration of doctoral studies in biochemistry, plant physiology and biophysics Structural and functional determinants on channels TRPC3, TRPV1, TRPV2 and TRPA1 Determination of Na+/K+-ATPase regulatory sites
http://linked.open...UplatneniVysledku	2009
http://linked.open...v/svazekPeriodika	1788
http://linked.open...iv/tvurceVysledku	Gryčová, Lenka Otyepka, Michal Teisinger, Jan Kubala, Martin Janovská, Marika Amler, Evžen Lánský, Zdeněk Sklenovský, Petr
http://linked.open...ain/vavai/riv/wos	000266190600019
http://linked.open...n/vavai/riv/zamer	Výzkum molekulárních a buněčných základů fyziologických a patofyziologických procesů s cílem objasnit mechanismy vzniku závažných onemocnění člověka Variabilita složek a interakcí v rostlinném patosystému a vliv faktorů prostředí na jejich projev Modulation of signalling and regulatory pathways in normal and cancer cells
issn	0005-2736
number of pages	11 (xsd:int)
http://localhost/t...ganizacniJednotka	15310
is http://linked.open...avai/riv/vysledek of	ATP and Magnesium Drive Conformational Changes of the Na+/K+-ATPase Cytoplasmic Headpiece ATP and Magnesium Drive Conformational Changes of the Na+/K+-ATPase Cytoplasmic Headpiece ATP and Magnesium Drive Conformational Changes of the Na+/K+-ATPase Cytoplasmic Headpiece ATP and Magnesium Drive Conformational Changes of the Na+/K+-ATPase Cytoplasmic Headpiece

Faceted Search & Find service v1.16.118 as of Jun 21 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 58 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software