5VIM
Crystal structure of the Zika virus NS5 methyltransferase.
Summary for 5VIM
| Entry DOI | 10.2210/pdb5vim/pdb |
| Descriptor | Methyltransferase, S-ADENOSYLMETHIONINE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | methyltransferase, zika virus, viral protein |
| Biological source | Zika virus (strain Mr 766) (ZIKV) |
| Cellular location | Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Lumenal side : A0A192GPS6 |
| Total number of polymer chains | 2 |
| Total formula weight | 59986.54 |
| Authors | Bukrejewska, M.,Derewenda, Z.S.,Derewenda, U. (deposition date: 2017-04-17, release date: 2017-09-06, Last modification date: 2023-10-04) |
| Primary citation | Bukrejewska, M.,Derewenda, U.,Radwanska, M.,Engel, D.A.,Derewenda, Z.S. Crystal structures of the methyltransferase and helicase from the ZIKA 1947 MR766 Uganda strain. Acta Crystallogr D Struct Biol, 73:767-774, 2017 Cited by PubMed Abstract: Two nonstructural proteins encoded by Zika virus strain MR766 RNA, a methyltransferase and a helicase, were crystallized and their structures were solved and refined at 2.10 and 2.01 Å resolution, respectively. The NS5 methyltransferase contains a bound S-adenosyl-L-methionine (SAM) co-substrate. The NS3 helicase is in the apo form. Comparison with published crystal structures of the helicase in the apo, nucleotide-bound and single-stranded RNA (ssRNA)-bound states suggests that binding of ssRNA to the helicase may occur through conformational selection rather than induced fit. PubMed: 28876240DOI: 10.1107/S2059798317010737 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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