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  Time-resolved crystallography reveals allosteric communication aligned with molecular breathing

Mehrabi, P., Schulz, E.-C., Dsouza, R., Müller-Werkmeister, H., Tellkamp, F., Miller, R. J. D., et al. (2019). Time-resolved crystallography reveals allosteric communication aligned with molecular breathing. Science, 365(6458), 1167-1170. doi:10.1126/science.aaw9904.

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Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-0004-ACDC-3 Versions-Permalink: https://hdl.handle.net/21.11116/0000-0005-1D9B-D
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PDF: Materials and Methods, Supplementary Text, Figs. S1 to S9, Table S1 Caption for Movie S1, References | MOVIE: All atom MD trajectory displaying FAc dynamics. Multiple conformations of FAc bound in the active site shown in a 10 ns all atom MD trajectory. The relative positions of FAc constantly modulate through time while periodically adopting states that match the crystallographic data (Fig. S4).
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https://dx.doi.org/10.1126/science.aaw9904 (Verlagsversion)
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 Urheber:
Mehrabi, P.1, 2, 3, Autor           
Schulz, E.-C.1, Autor           
Dsouza, R.1, 4, Autor           
Müller-Werkmeister, H.1, 5, Autor           
Tellkamp, F.6, Autor           
Miller, R. J. D.1, 7, Autor           
Pai, E. F.2, 3, 8, Autor
Affiliations:
1Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_1938288              
2Department of Medical Biophysics, University of Toronto, ou_persistent22              
3The Campbell Family Cancer Research Institute, Ontario Cancer Institute, ou_persistent22              
4Department of Physics, University of Hamburg, ou_persistent22              
5Institute of Chemistry - Physical Chemistry, University of Potsdam, ou_persistent22              
6Machine Physics, Scientific Service Units, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_2074322              
7Departments of Chemistry and Physics, University of Toronto, ou_persistent22              
8Departments of Biochemistry and Molecular Genetics, University of Toronto, ou_persistent22              

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 Zusammenfassung: A comprehensive understanding of protein function demands correlating structure and dynamic changes. Using time-resolved serial synchrotron crystallography, we visualized half-of-the-sites reactivity and correlated molecular-breathing motions in the enzyme fluoroacetate dehalogenase. Eighteen time points from 30 milliseconds to 30 seconds cover four turnover cycles of the irreversible reaction. They reveal sequential substrate binding, covalent-intermediate formation, setup of a hydrolytic water molecule, and product release. Small structural changes of the protein mold and variations in the number and placement of water molecules accompany the various chemical steps of catalysis. Triggered by enzyme-ligand interactions, these repetitive changes in the protein framework’s dynamics and entropy constitute crucial components of the catalytic machinery.

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Sprache(n): eng - English
 Datum: 2019-02-122019-08-212019-09-132019-09-13
 Publikationsstatus: Erschienen
 Seiten: 4
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1126/science.aaw9904
 Art des Abschluß: -

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Projektname : Support was provided by the Max Planck Society and by the Cluster of Excellence “The Hamburg Centre for Ultrafast Imaging” of the Deutsche Forschungsgemeinschaft (DFG) - EXC 1074 - project ID 194651731 (R.J.D.M.), the People Programme (Marie Curie Actions) of the European Union’s Seventh Framework Programme (FP7/2007–2013) under REA grant no. 623994 (H.M.M.-W.), the Natural Sciences and Engineering Research Council of Canada (RGPIN-2015-04877), the Canada Research Chairs program, and the Burroughs Wellcome Fund via a Collaborative Research Travel Grant (E.F.P.). P.M. was the recipient of an Alexander von Humboldt-Stiftung postdoctoral research award.
Grant ID : 623994
Förderprogramm : Funding Programme 7 (FP7)
Förderorganisation : European Commission (EC)

Quelle 1

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Titel: Science
  Andere : Science
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Washington, D.C. : American Association for the Advancement of Science
Seiten: - Band / Heft: 365 (6458) Artikelnummer: - Start- / Endseite: 1167 - 1170 Identifikator: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1