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Octahedral trifluoromagnesate, an anomalous metal fluoride species, stabilizes the transition state in a biological motor

DOI: 10.1021/acscatal.0c04500 DOI Help

Authors: Mengyu Ge (University of York) , Robert W. Molt (ndiana University School of Medicine; ENSCO, Inc) , Huw T. Jenkins (University of York) , G. Michael Blackburn (University of Sheffield) , Yi Jin (Cardiff University) , Alfred A. Antson (University of York)
Co-authored by industrial partner: Yes

Type: Journal Paper
Journal: Acs Catalysis

State: Published (Approved)
Published: February 2021
Diamond Proposal Number(s): 13587

Open Access Open Access

Abstract: Isoelectronic metal fluoride transition state analogue (TSA) complexes, MgF3– and AlF4–, have proven to be immensely useful in understanding mechanisms of biological motors utilizing phosphoryl transfer. Here we report a previously unobserved octahedral TSA complex, MgF3(H2O)−, in a 1.5 Å resolution Zika virus NS3 helicase crystal structure. 19F NMR provided independent validation and also the direct observation of conformational tightening resulting from ssRNA binding in solution. The TSA stabilizes the two conformations of motif V of the helicase that link ATP hydrolysis with mechanical work. DFT analysis further validated the MgF3(H2O)− species, indicating the significance of this TSA for studies of biological motors.

Journal Keywords: virus helicase; transition state analogue; ATPase; 19F NMR; protein crystallography; general base catalysis; phosphoryl transfer mechanism

Subject Areas: Chemistry, Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography

Documents:
acscatal.0c04500.pdf

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