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TitleStructural and functional basis of low-affinity SAM/SAH-binding in the conserved MTase of the multi-segmented Alongshan virus distantly related to canonical unsegmented flaviviruses.
Journal, issue, pagesPlos Pathog., Vol. 19, Page e1011694-e1011694, Year 2023
Publish dateSep 21, 2022 (structure data deposition date)
AuthorsChen, H. / Lin, S. / Yang, F. / Chen, Z. / Guo, L. / Yang, J. / Lin, X. / Wang, L. / Duan, Y. / Wen, A. ...Chen, H. / Lin, S. / Yang, F. / Chen, Z. / Guo, L. / Yang, J. / Lin, X. / Wang, L. / Duan, Y. / Wen, A. / Zhang, X. / Dai, Y. / Yin, K. / Yuan, X. / Yu, C. / He, Y. / He, B. / Cao, Y. / Dong, H. / Li, J. / Zhao, Q. / Liu, Q. / Lu, G.
External linksPlos Pathog. / PubMed:37831643
MethodsX-ray diffraction
Resolution2.005 - 2.5 Å
Structure data

PDB-8gy4:
Crystal structure of Alongshan virus methyltransferase
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-8gy9:
Crystal structure of Alongshan virus methyltransferase bound to S-adenosyl-L-methionine
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-8gya:
Crystal structure of Alongshan virus methyltransferase bound to Sinefungin
Method: X-RAY DIFFRACTION / Resolution: 2.005 Å

PDB-8gyb:
Crystal structure of Alongshan virus methyltransferase bound to S-adenosyl-L-homocysteine
Method: X-RAY DIFFRACTION / Resolution: 2.101 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-SAM:
S-ADENOSYLMETHIONINE

ChemComp-SFG:
SINEFUNGIN

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

Source
  • alongshan virus
KeywordsVIRAL PROTEIN / Methyltransferase

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