Journal
SCIENCE
Volume 365, Issue 6458, Pages 1167-+Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aaw9904
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Funding
- Max Planck Society
- Cluster of Excellence The Hamburg Centre for Ultrafast Imaging of the Deutsche Forschungsgemeinschaft (DFG) [EXC 1074, 194651731]
- European Union [623994]
- Natural Sciences and Engineering Research Council of Canada [RGPIN-2015-04877]
- Canada Research Chairs program
- Burroughs Wellcome Fund
- Alexander von Humboldt-Stiftung
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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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