5K8L: Apo structure

Zika virus has attracted increasing attention because of its potential for causing human neural disorders, including microcephaly in infants and Guillain-Barre syndrome. Its NS3 helicase domain plays critical roles in NTP-dependent RNA unwinding and translocation during viral replication. Our structural analysis revealed a pre-activation state of NS3 helicase in complex with GTPgammaS, in which the triphosphate adopts a compact conformation in the absence of any divalent metal ions. In contrast, in the presence of a divalent cation, GTPgammaS adopts an extended conformation, and the Walker A motif undergoes substantial conformational changes. Both features contribute to more extensive interactions between the GTPgammaS and the enzyme. Thus, this study provides structural evidence on the allosteric modulation of MgNTP(2-) on the NS3 helicase activity. Furthermore, the compact conformation of inhibitory NTP identified in this study provides precise information for the rational drug design of small molecule inhibitors for the treatment of ZIKV infection.
PDB ID: 5K8LDownload
MMDB ID: 144751
PDB Deposition Date: 2016/5/30
Updated in MMDB: 2017/12
Experimental Method:
x-ray diffraction
Resolution: 1.751  Å
Source Organism:
Similar Structures:
Biological Unit for 5K8L: monomeric; determined by author
Molecular Components in 5K8L
Label Count Molecule
Protein (1 molecule)
Zikv NS3 Helicase
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB