5ULP
Structure of the NS5 methyltransferase from Zika bound to MS2042
Summary for 5ULP
| Entry DOI | 10.2210/pdb5ulp/pdb |
| Related | 5KQR 5KQS |
| Descriptor | MRNA cap 0-1 NS5-type methyltransferase, 5'-{[(3S)-3-amino-3-carboxypropyl][(4-fluorophenyl)methyl]amino}-5'-deoxyadenosine, CHLORIDE ION, ... (7 entities in total) |
| Functional Keywords | zika, flavivirus, ns5, methyltransferase, ms2042, sam analog, hydrolase |
| Biological source | Zika virus (strain Mr 766) (ZIKV) |
| Cellular location | Virion membrane ; Multi-pass membrane protein : B3U3M3 |
| Total number of polymer chains | 2 |
| Total formula weight | 60840.92 |
| Authors | Jain, R.,Aggarwal, A.K. (deposition date: 2017-01-25, release date: 2017-05-17, Last modification date: 2024-11-20) |
| Primary citation | Jain, R.,Butler, K.V.,Coloma, J.,Jin, J.,Aggarwal, A.K. Development of a S-adenosylmethionine analog that intrudes the RNA-cap binding site of Zika methyltransferase. Sci Rep, 7:1632-1632, 2017 Cited by PubMed Abstract: The Zika virus (ZIKV) has emerged as a major health hazard. We present here a high resolution structure (1.55 Å) of ZIKV NS5 methyltransferase bound to a novel S-adenosylmethionine (SAM) analog in which a 4-fluorophenyl moiety substitutes for the methyl group. We show that the 4-fluorophenyl moiety extends into a portion of the RNA binding tunnel that typically contains the adenosine 2'OH of the RNA-cap moiety. Together, the new SAM analog and the high-resolution crystal structure are a step towards the development of antivirals against ZIKV and other flaviviruses. PubMed: 28487506DOI: 10.1038/s41598-017-01756-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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