6S0J

Structure of Zika virus NS3 helicase in complex with ADP-MgF3(H2O)-

Summary for 6S0J

• Entry DOI: 10.2210/pdb6s0j/pdb
• Descriptor: Genome polyprotein, trifluoromagnesate monohydrate, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: ns3 helicase, hydrolase
• Biological source: Zika virus (strain Mr 766)
• Total number of polymer chains: 1
• Total formula weight: 51293.69

Authors

Ge, M.,Molt Jr., R.W.,Jenkins, H.T.,Blackburn, G.M.,Jin, Y.,Antson, A.A. (deposition date: 2019-06-16, release date: 2020-07-15, Last modification date: 2025-11-19)

Primary citation

Ge, M.,Molt Jr., R.W.,Jenkins, H.T.,Blackburn, G.M.,Jin, Y.,Antson, A.A.
Octahedral Trifluoromagnesate, an Anomalous Metal Fluoride Species, Stabilizes the Transition State in a Biological Motor.
Acs Catalysis, 11:2769-2773, 2021

PubMed Abstract: Isoelectronic metal fluoride transition state analogue (TSA) complexes, MgF and AlF , 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(HO), in a 1.5 Å resolution Zika virus NS3 helicase crystal structure. 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(HO) species, indicating the significance of this TSA for studies of biological motors.

PubMed: 33717640
DOI: 10.1021/acscatal.0c04500

Experimental method

X-RAY DIFFRACTION (1.5 Å)