5H4I

Unlinked NS2B-NS3 Protease from Zika Virus in complex with a compound fragment

Summary for 5H4I

• Entry DOI: 10.2210/pdb5h4i/pdb
• Descriptor: NS2B cofactor, NS3 protease, benzimidazol-1-ylmethanol, ... (5 entities in total)
• Functional Keywords: zika virus protease, serine protease, non-structural protein 3, viral protein
• Biological source: Zika virus; More
• Total number of polymer chains: 2
• Total formula weight: 25096.16

Authors

Zhang, Z.Z.,Li, Y. (deposition date: 2016-10-31, release date: 2016-12-14, Last modification date: 2023-11-08)

Primary citation

Zhang, Z.,Li, Y.,Loh, Y.R.,Phoo, W.W.,Hung, A.W.,Kang, C.,Luo, D.
Crystal structure of unlinked NS2B-NS3 protease from Zika virus
Science, 354:1597-1600, 2016

PubMed Abstract: Zika virus (ZIKV) has rapidly emerged as a global public health concern. Viral NS2B-NS3 protease processes viral polyprotein and is essential for the virus replication, making it an attractive antiviral drug target. We report crystal structures at 1.58-angstrom resolution of the unlinked NS2B-NS3 protease from ZIKV as free enzyme and bound to a peptide reversely oriented at the active site. The unlinked NS2B-NS3 protease adopts a closed conformation in which NS2B engages NS3 to form an empty substrate-binding site. A second protease in the same crystal binds to the residues K14K15G16E17 from the neighboring NS3 in reverse orientation, resisting proteolysis. These features of ZIKV NS2B-NS3 protease may accelerate the discovery of structure-based antiviral drugs against ZIKV and related pathogenic flaviviruses.

PubMed: 27940580
DOI: 10.1126/science.aai9309

Experimental method

X-RAY DIFFRACTION (2.004 Å)