Time-resolved crystallography reveals allosteric communication aligned with molecular breathing
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Time-resolved crystallography reveals allosteric communication aligned with molecular breathing. / Mehrabi, Pedram; Schulz, Eike C; Dsouza, Raison; Müller-Werkmeister, Henrike M; Tellkamp, Friedjof; Miller, R J Dwayne; Pai, Emil F.
in: SCIENCE, Jahrgang 365, Nr. 6458, 13.09.2019, S. 1167-1170.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Time-resolved crystallography reveals allosteric communication aligned with molecular breathing
AU - Mehrabi, Pedram
AU - Schulz, Eike C
AU - Dsouza, Raison
AU - Müller-Werkmeister, Henrike M
AU - Tellkamp, Friedjof
AU - Miller, R J Dwayne
AU - Pai, Emil F
N1 - Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.
PY - 2019/9/13
Y1 - 2019/9/13
N2 - 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.
AB - 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.
KW - Bacterial Proteins/chemistry
KW - Catalysis
KW - Catalytic Domain
KW - Entropy
KW - Hydrolases/chemistry
KW - Kinetics
KW - Ligands
KW - Models, Molecular
KW - Protein Conformation
KW - Protein Multimerization
KW - Rhodopseudomonas/enzymology
U2 - 10.1126/science.aaw9904
DO - 10.1126/science.aaw9904
M3 - SCORING: Journal article
C2 - 31515393
VL - 365
SP - 1167
EP - 1170
JO - SCIENCE
JF - SCIENCE
SN - 0036-8075
IS - 6458
ER -