DC Element | Wert | Sprache |
dc.contributor.author | Shalaeva, Daria N. | |
dc.contributor.author | Cherepanov, Dmitry A. | |
dc.contributor.author | Galperin, Michael Y. | |
dc.contributor.author | Golovin, Andrey V. | |
dc.contributor.author | Mulkidjanian, Armen Y. | |
dc.date.accessioned | 2021-12-23T16:21:32Z | - |
dc.date.available | 2021-12-23T16:21:32Z | - |
dc.date.issued | 2018 | |
dc.identifier.issn | 2050084X | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/13910 | - |
dc.description.abstract | The ubiquitous P-loop fold nucleoside triphosphatases (NTPases) are typically activated by an arginine or lysine `finger'. Some of the apparently ancestral NTPases are, instead, activated by potassium ions. To clarify the activation mechanism, we combined comparative structure analysis with molecular dynamics (MD) simulations of Mg-ATP and Mg-GTP complexes in water and in the presence of potassium, sodium, or ammonium ions. In all analyzed structures of diverse P-loop NTPases, the conserved P-loop motif keeps the triphosphate chain of bound NTPs (or their analogs) in an extended, catalytically prone conformation, similar to that imposed on NTPs in water by potassium or ammonium ions. MD simulations of potassium-dependent GTPase MnmE showed that linking of alpha- and gamma phosphates by the activating potassium ion led to the rotation of the gamma-phosphate group yielding an almost eclipsed, catalytically productive conformation of the triphosphate chain, which could represent the basic mechanism of hydrolysis by P-loop NTPases. | |
dc.description.sponsorship | Deutscher Akademischer AustauschdienstDeutscher Akademischer Austausch Dienst (DAAD); Russian Science FoundationRussian Science Foundation (RSF) [14-50-00029]; U.S. National Library of MedicineUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Library of Medicine (NLM); Lomonosov Moscow State University [RFMEFI62117X0011]; Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [DFG-436-RUS 113/963/0-1]; Bundesministerium fur Bildung und ForschungFederal Ministry of Education & Research (BMBF); Osnabrueck University; Deutscher Akademischer Austauschdienst Ostpartnerschaften programm Daria N Shalaeva; Russian Science Foundation 14-50-00029 (Noah's Ark) Daria N Shalaeva Dmitry A Cherepanov Andrey V Golovin; U.S. National Library of Medicine Intramural Research Program Michael Y Galperin; Lomonosov Moscow State University RFMEFI62117X0011 Andrey V Golovin; Deutsche Forschungsgemeinschaft DFG-436-RUS 113/963/0-1 Armen Y Mulkidjanian; Bundesministerium fur Bildung und Forschung Laseromix Armen Y Mulkidjanian; Osnabrueck University EvoCell Program Armen Y Mulkidjanian; The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication. | |
dc.language.iso | en | |
dc.publisher | ELIFE SCIENCES PUBLICATIONS LTD | |
dc.relation.ispartof | ELIFE | |
dc.subject | 16S RIBOSOMAL-RNA | |
dc.subject | ATP HYDROLYSIS | |
dc.subject | Biology | |
dc.subject | ELONGATION-FACTOR TU | |
dc.subject | ESCHERICHIA-COLI | |
dc.subject | FORCE-FIELD | |
dc.subject | G DOMAIN | |
dc.subject | GTPASE ACTIVITY | |
dc.subject | Life Sciences & Biomedicine - Other Topics | |
dc.subject | MOLECULAR-DYNAMICS SIMULATION | |
dc.subject | PHOSPHORYL TRANSFER | |
dc.subject | STRUCTURAL BASIS | |
dc.title | Evolution of cation binding in the active sites of P-loop nucleoside triphosphatases in relation to the basic catalytic mechanism | |
dc.type | journal article | |
dc.identifier.doi | 10.7554/eLife.37373 | |
dc.identifier.isi | ISI:000454486300001 | |
dc.description.volume | 7 | |
dc.contributor.orcid | 0000-0002-2265-5572 | |
dc.contributor.orcid | 0000-0001-5844-3064 | |
dc.contributor.orcid | 0000-0001-6286-4638 | |
dc.contributor.orcid | 0000-0003-0582-2612 | |
dc.contributor.orcid | 0000-0002-8908-4268 | |
dc.contributor.researcherid | B-5859-2013 | |
dc.contributor.researcherid | AAH-3608-2021 | |
dc.contributor.researcherid | J-8086-2013 | |
dc.contributor.researcherid | R-8391-2016 | |
dc.contributor.researcherid | ABB-4382-2020 | |
dc.publisher.place | SHERATON HOUSE, CASTLE PARK, CAMBRIDGE, CB3 0AX, ENGLAND | |
dcterms.isPartOf.abbreviation | eLife | |
dcterms.oaStatus | Green Submitted, Green Published, gold | |