5TFR

Crystal structure of Zika Virus NS5 protein

Summary for 5TFR

• Entry DOI: 10.2210/pdb5tfr/pdb
• Descriptor: Genome polyprotein, S-ADENOSYL-L-HOMOCYSTEINE, ZINC ION, ... (4 entities in total)
• Functional Keywords: mtase, methyltransferase, polymerase, rdrp, rna-dependent rna polymerase, flavivirus, zika, viral protein
• Biological source: Zika virus (strain Mr 766) (ZIKV)
• Cellular location: Capsid protein C: Virion . Peptide pr: Secreted . Small envelope protein M: Virion membrane ; Multi-pass membrane protein . Envelope protein E: Virion membrane ; Multi-pass membrane protein . Non-structural protein 1: Secreted . Non-structural protein 2A: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Multi-pass membrane protein . Serine protease NS3: Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side . Non-structural protein 4A: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Non-structural protein 4B: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side: Q32ZE1
• Total number of polymer chains: 2
• Total formula weight: 208186.90

Authors

Longenecker, K.L.,Upadhyay, A.K. (deposition date: 2016-09-26, release date: 2016-10-12, Last modification date: 2023-10-04)

Primary citation

Upadhyay, A.K.,Cyr, M.,Longenecker, K.,Tripathi, R.,Sun, C.,Kempf, D.J.
Crystal structure of full-length Zika virus NS5 protein reveals a conformation similar to Japanese encephalitis virus NS5.
Acta Crystallogr F Struct Biol Commun, 73:116-122, 2017

PubMed Abstract: The rapid spread of the recent Zika virus (ZIKV) epidemic across various countries in the American continent poses a major health hazard for the unborn fetuses of pregnant women. To date, there is no effective medical intervention. The nonstructural protein 5 of Zika virus (ZIKV-NS5) is critical for ZIKV replication through the 5'-RNA capping and RNA polymerase activities present in its N-terminal methyltransferase (MTase) and C-terminal RNA-dependent RNA polymerase (RdRp) domains, respectively. The crystal structure of the full-length ZIKV-NS5 protein has been determined at 3.05 Å resolution from a crystal belonging to space group P222 and containing two protein molecules in the asymmetric unit. The structure is similar to that reported for the NS5 protein from Japanese encephalitis virus and suggests opportunities for structure-based drug design targeting either its MTase or RdRp domain.

PubMed: 28291746
DOI: 10.1107/S2053230X17001601

Experimental method

X-RAY DIFFRACTION (3.05 Å)