{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T01:10:25Z","timestamp":1790730625435,"version":"4.1.0"},"reference-count":137,"publisher":"MDPI AG","issue":"22","license":[{"start":{"date-parts":[[2020,11,12]],"date-time":"2020-11-12T00:00:00Z","timestamp":1605139200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003006","name":"Eidgen\u00f6ssische Technische Hochschule Z\u00fcrich","doi-asserted-by":"publisher","award":["SEED-69 16-1"],"award-info":[{"award-number":["SEED-69 16-1"]}],"id":[{"id":"10.13039\/501100003006","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003006","name":"Eidgen\u00f6ssische Technische Hochschule Z\u00fcrich","doi-asserted-by":"publisher","award":["ETH-43 17-2"],"award-info":[{"award-number":["ETH-43 17-2"]}],"id":[{"id":"10.13039\/501100003006","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000781","name":"European Research Council","doi-asserted-by":"publisher","award":["741863"],"award-info":[{"award-number":["741863"]}],"id":[{"id":"10.13039\/501100000781","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Schweizerischer Nationalfonds zur F&amp;#x00F6;rderung der Wissenschaftlichen Forschung","award":["200020_159707"],"award-info":[{"award-number":["200020_159707"]}]},{"name":"Schweizerischer Nationalfonds zur F&amp;#x00F6;rderung der Wissenschaftlichen Forschung","award":["200020-188711"],"award-info":[{"award-number":["200020-188711"]}]},{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-14-CE09-0024B"],"award-info":[{"award-number":["ANR-14-CE09-0024B"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-19-CE11-0023"],"award-info":[{"award-number":["ANR-19-CE11-0023"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100018873","name":"LABEX ECOFECT","doi-asserted-by":"publisher","award":["ANR-11-LABX-0048"],"award-info":[{"award-number":["ANR-11-LABX-0048"]}],"id":[{"id":"10.13039\/501100018873","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100018873","name":"LABEX ECOFECT","doi-asserted-by":"publisher","award":["ANR-11-IDEX-0007"],"award-info":[{"award-number":["ANR-11-IDEX-0007"]}],"id":[{"id":"10.13039\/501100018873","id-type":"DOI","asserted-by":"publisher"}]},{"name":"EvoCell Program of the Osnabrueck University","award":["xxx"],"award-info":[{"award-number":["xxx"]}]},{"DOI":"10.13039\/501100006769","name":"Russian Science Foundation","doi-asserted-by":"publisher","award":["17-14-01314"],"award-info":[{"award-number":["17-14-01314"]}],"id":[{"id":"10.13039\/501100006769","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Nucleoside triphosphates (NTPs) are used as chemical energy source in a variety of cell systems. Structural snapshots along the NTP hydrolysis reaction coordinate are typically obtained by adding stable, nonhydrolyzable adenosine triphosphate (ATP) -analogues to the proteins, with the goal to arrest a state that mimics as closely as possible a physiologically relevant state, e.g., the pre-hydrolytic, transition and post-hydrolytic states. We here present the lessons learned on two distinct ATPases on the best use and unexpected pitfalls observed for different analogues. The proteins investigated are the bacterial DnaB helicase from Helicobacter pylori and the multidrug ATP binding cassette (ABC) transporter BmrA from Bacillus subtilis, both belonging to the same division of P-loop fold NTPases. We review the magnetic-resonance strategies which can be of use to probe the binding of the ATP-mimics, and present carbon-13, phosphorus-31, and vanadium-51 solid-state nuclear magnetic resonance (NMR) spectra of the proteins or the bound molecules to unravel conformational and dynamic changes upon binding of the ATP-mimics. Electron paramagnetic resonance (EPR), and in particular W-band electron-electron double resonance (ELDOR)-detected NMR, is of complementary use to assess binding of vanadate. We discuss which analogues best mimic the different hydrolysis states for the DnaB helicase and the ABC transporter BmrA. These might be relevant also to structural and functional studies of other NTPases.<\/jats:p>","DOI":"10.3390\/molecules25225268","type":"journal-article","created":{"date-parts":[[2020,11,12]],"date-time":"2020-11-12T20:17:52Z","timestamp":1605212272000},"page":"5268","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":59,"title":["ATP Analogues for Structural Investigations: Case Studies of a DnaB Helicase and an ABC Transporter"],"prefix":"10.3390","volume":"25","author":[{"given":"Denis","family":"Lacabanne","sequence":"first","affiliation":[{"name":"Laboratory of Physical Chemistry, ETH Zurich, 8093 Zurich, Switzerland"},{"name":"Medical Research Council Mitochondrial Biology Unit University of Cambridge, Cambridge Biomedical Campus, Keith Peters Building, Hills Road, Cambridge CB2 0XY, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3655-6150","authenticated-orcid":false,"given":"Thomas","family":"Wiegand","sequence":"additional","affiliation":[{"name":"Laboratory of Physical Chemistry, ETH Zurich, 8093 Zurich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4890-3842","authenticated-orcid":false,"given":"Nino","family":"Wili","sequence":"additional","affiliation":[{"name":"Laboratory of Physical Chemistry, ETH Zurich, 8093 Zurich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0699-5064","authenticated-orcid":false,"given":"Maria I.","family":"Kozlova","sequence":"additional","affiliation":[{"name":"Department of Physics, Osnabrueck University, 49069 Osnabrueck, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Riccardo","family":"Cadalbert","sequence":"additional","affiliation":[{"name":"Laboratory of Physical Chemistry, ETH Zurich, 8093 Zurich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel","family":"Klose","sequence":"additional","affiliation":[{"name":"Laboratory of Physical Chemistry, ETH Zurich, 8093 Zurich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Armen Y.","family":"Mulkidjanian","sequence":"additional","affiliation":[{"name":"Department of Physics, Osnabrueck University, 49069 Osnabrueck, Germany"},{"name":"School of Bioengineering and Bioinformatics and Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119234 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Beat H.","family":"Meier","sequence":"additional","affiliation":[{"name":"Laboratory of Physical Chemistry, ETH Zurich, 8093 Zurich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anja","family":"B\u00f6ckmann","sequence":"additional","affiliation":[{"name":"Molecular Microbiology and Structural Biochemistry UMR 5086 CNRS\/Universit\u00e9 de Lyon, Labex Ecofect, 69367 Lyon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,11,12]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1534","DOI":"10.1039\/C9CP02194A","article-title":"Mechanistic study of the ATP hydrolysis reaction in dynein motor protein","volume":"22","author":"Manna","year":"2020","journal-title":"Phys. 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