Octahedral Trifluoromagnesate, an Anomalous Metal Fluoride Species, Stabilizes the Transition State in a Biological Motor | Zendy

Mengyu Ge | Zendy; Robert W. Molt | Zendy; Huw T. Jenkins | Zendy; G. Michael Blackburn | Zendy; Yi Jin | Zendy; Alfred A. Antson | Zendy

Open Access

Octahedral Trifluoromagnesate, an Anomalous Metal Fluoride Species, Stabilizes the Transition State in a Biological Motor

Author(s) -

Mengyu Ge,

Robert W. Molt,

Huw T. Jenkins,

G. Michael Blackburn,

Yi Jin,

Alfred A. Antson

Publication year - 2021

Publication title -

acs catalysis

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 4.898

H-Index - 198

ISSN - 2155-5435

DOI - 10.1021/acscatal.0c04500

Subject(s) - helicase , chemistry , octahedron , atp hydrolysis , fluoride , crystallography , transition metal , metal , crystal structure , catalysis , enzyme , inorganic chemistry , organic chemistry , atpase , rna , biochemistry , gene

Isoelectronic metal fluoride transition state analogue (TSA) complexes, MgF 3 - and AlF 4 - , have proven to be immensely useful in understanding mechanisms of biological motors utilizing phosphoryl transfer. Here we report a previously unobserved octahedral TSA complex, MgF 3 (H 2 O) - , in a 1.5 Å resolution Zika virus NS3 helicase crystal structure. 19 F 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 MgF 3 (H 2 O) - species, indicating the significance of this TSA for studies of biological motors.

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