Time-resolved crystallography reveals allosteric communication aligned with molecular breathing-Reference-Cited by-同舟云学术

Time-resolved crystallography reveals allosteric communication aligned with molecular breathing

Published:2019-09-13 Issue:6458 Volume:365 Page:1167-1170
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Mehrabi Pedram¹²³^ORCID,Schulz Eike C.¹^ORCID,Dsouza Raison¹⁴^ORCID,Müller-Werkmeister Henrike M.¹⁵^ORCID,Tellkamp Friedjof⁶^ORCID,Miller R. J. Dwayne¹⁷^ORCID,Pai Emil F.²³⁸^ORCID

Affiliation:

1. Department for Atomically Resolved Dynamics, Max-Planck-Institute for Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany.

2. Department of Medical Biophysics, University of Toronto, 101 College Street, Toronto, Ontario M5G 1L7, Canada.

3. The Campbell Family Cancer Research Institute, Ontario Cancer Institute, 101 College Street, Toronto, Ontario M5G 1L7, Canada.

4. Department of Physics, University of Hamburg, Jungiusstrasse 9, 20355 Hamburg, Germany.

5. Institute of Chemistry - Physical Chemistry, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Potsdam-Golm, Germany.

6. Scientific Support Unit Machine Physics, Max-Planck-Institute for Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany.

7. Departments of Chemistry and Physics, University of Toronto, 80 St. George Street, Toronto, Ontario M5S 3H6, Canada.

8. Departments of Biochemistry and Molecular Genetics, University of Toronto, 1 King’s College Circle, Toronto, Ontario M5S 1A8, Canada.

Abstract

Active sites that move together Enzymes often form dimers or higher-order oligomers, even when each active site is isolated and the reactions are simple. But the effect of a neighbor can be profound. Mehrabi et al. used a photolabile compound to initiate a reaction in the enzyme fluoroacetate dehalogenase, which they could follow by time-resolved serial synchrotron crystallography. Snapshots of the reaction revealed coupled allosteric motions between the two active sites of the dimeric enzyme. Each active site traded the ability to bind substrate and catalyze the reaction, such that only one was engaged at a time. This behavior is common in enzymes but is rarely visualized and still poorly understood. Science , this issue p. 1167

Funder

Alexander von Humboldt-Stiftung

Canada Research Chairs

National Sciences and Engineering Research Council of Canada

People Programme (Marie Curie Actions) of the European Union’s Seventh Framework Programme

Center for Ultrafast Imaging - Structure, Dynamics and Control of Matter at the atomic scale of the Deutsche Forschungsgemeinschaft

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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