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Computer modelling reveals new conformers of the ATP binding loop of Na+/K+-ATPase involved in the transphosphorylation process of the sodium pump
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SYSNO ASEP 0477214 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Computer modelling reveals new conformers of the ATP binding loop of Na+/K+-ATPase involved in the transphosphorylation process of the sodium pump Tvůrce(i) Tejral, Gracian (UEM-P)
Sopko, B. (CZ)
Nečas, A. (CZ)
Schoner, W. (DE)
Amler, Evžen (UEM-P) RIDZdroj.dok. PeerJ. - : PeerJ - ISSN 2167-8359
Roč. 5, mar (2017), s. 3087Poč.str. 22 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova M4M5 loop ; open and closed conformations ; hinge movement ; Na+/K+-ATPase phosphorylation Vědní obor RIV EB - Genetika a molekulární biologie Obor OECD Biology (theoretical, mathematical, thermal, cryobiology, biological rhythm), Evolutionary biology CEP GA15-15697S GA ČR - Grantová agentura ČR LO1508 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy LO1309 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Institucionální podpora UEM-P - RVO:68378041 UT WOS 000396906100007 EID SCOPUS 85015203992 DOI https://doi.org/10.7717/peerj.3087 Anotace Hydrolysis of ATP by Na+/K+-ATPase, a P-Type ATPase, catalyzing active Na+ and K+ transport through cellular membranes leads transiently to a phosphorylation of its catalytical alpha-subunit. Surprisingly, three-dimensional molecular structure analysis of P-type ATPases reveals that binding of ATP to the N-domain connected by a hinge to the P-domain is much too far away from the Asp(369) to allow the transfer of ATP's terminal phosphate to its aspartyl-phosphorylation site. In order to get information for how the transfer of the gamma-phosphate group of ATP to the Asp(369) is achieved, analogous molecular modeling of the M-4 M-5 loop of ATPase was performed using the crystal data of Na+/K+-ATPase of different species. Analogous molecular modeling of the cytoplasmic loop between Thr(338) and Ile(760) of the a alpha-subunit of Na+/K+-ATPase and the analysis of distances between the ATP binding site and phosphorylation site revealed the existence of two ATP binding sites in the open conformation, the first one close to Phe(475) in the N-domain, the other one close to Asp(369) in the 13-domain. However, binding of Mg2+circle ATP to any of these sites in the open conformation may not lead to phosphorylation of Asp(369). Additional conformations of the cytoplasmic loop were found wobbling between open conformation == semi-open conformation == closed conformation in the absence of 2Mg(2+)circle ATP. The cytoplasmic loop's conformational change to the semi-open conformatio characterized by a hydrogen bond between Arg(543) and Asp(611) triggers by binding of 2Mg(2+)circle ATP Ito a single ATP l site and conversion to the closed l conformation the phosphorylation of Asp(369) in the P-domain, and hence the start of Na+/K+-activated ATP hydrolysis. Pracoviště Ústav experimentální medicíny Kontakt Arzuv Čaryjeva, arzuv.caryjeva@iem.cas.cz, Tel.: 241 062 218, 296 442 218 Rok sběru 2018
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