5KQR

Structure of NS5 methyltransferase from Zika virus bound to S-adenosylmethionine

Summary for 5KQR

• Entry DOI: 10.2210/pdb5kqr/pdb
• Descriptor: Methyltransferase, S-ADENOSYLMETHIONINE, PHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: zika, flavivirus, transferase
• Biological source: Zika virus (ZIKV)
• Cellular location: Virion membrane ; Multi-pass membrane protein : H9A910
• Total number of polymer chains: 1
• Total formula weight: 30067.60

Authors

Jain, R.,Coloma, J.,Rajashankar, K.R.,Aggarwal, A.K. (deposition date: 2016-07-06, release date: 2016-09-14, Last modification date: 2023-10-04)

Primary citation

Coloma, J.,Jain, R.,Rajashankar, K.R.,Garcia-Sastre, A.,Aggarwal, A.K.
Structures of NS5 Methyltransferase from Zika Virus.
Cell Rep, 16:3097-3102, 2016

PubMed Abstract: The Zika virus (ZIKV) poses a major public health emergency. To aid in the development of antivirals, we present two high-resolution crystal structures of the ZIKV NS5 methyltransferase: one bound to S-adenosylmethionine (SAM) and the other bound to SAM and 7-methyl guanosine diphosphate (7-MeGpp). We identify features of ZIKV NS5 methyltransferase that lend to structure-based antiviral drug discovery. Specifically, SAM analogs with functionalities on the Cβ atom of the methionine portion of the molecules that occupy the RNA binding tunnel may provide better specificity relative to human RNA methyltransferases.

PubMed: 27633330
DOI: 10.1016/j.celrep.2016.08.091

Experimental method

X-RAY DIFFRACTION (1.331 Å)