3gcz Citations

Crystal structure of a methyltransferase from a no-known-vector Flavivirus.

Biochem. Biophys. Res. Commun. 382 200-4 (2009)
Cited: 9 times
EuropePMC logo PMID: 19275894


Presently known flaviviruses belong to three major evolutionary branches: tick-borne viruses, mosquito-borne viruses and viruses with no known vector. Here we present the crystal structure of the Yokose virus methyltransferase at 1.7A resolution, the first structure of a methyltransferase of a Flavivirus with no known vector. Structural comparison of three methyltransferases representative of each of the Flavivirus branches shows that fold and structures are closely conserved, most differences being related to surface loops flexibility. Analysis of the conserved residues throughout all the sequenced flaviviral methyltransferases reveals that, besides the central cleft hosting the substrate and cofactor binding sites, a second, almost continuous, patch is conserved and points away from active site towards the back of the protein. The high level of structural conservation in this region could be functional for the methyltransferase/RNA interaction and stabilization of the ensuing complex.

Articles - 3gcz mentioned but not cited (1)

Reviews citing this publication (2)

  1. A Review of Flaviviruses that Have No Known Arthropod Vector. Blitvich BJ, Firth AE. Viruses 9 (2017)
  2. Structure and functionality in flavivirus NS-proteins: perspectives for drug design. Bollati M, Alvarez K, Assenberg R, Baronti C, Canard B, Cook S, Coutard B, Decroly E, de Lamballerie X, Gould EA, Grard G, Grimes JM, Hilgenfeld R, Jansson AM, Malet H, Mancini EJ, Mastrangelo E, Mattevi A, Milani M, Moureau G, Neyts J, Owens RJ, Ren J, Selisko B, Speroni S, Steuber H, Stuart DI, Unge T, Bolognesi M. Antiviral Res. 87 125-148 (2010)

Articles citing this publication (6)

  1. Dengue virus nonstructural protein 5 adopts multiple conformations in solution. Bussetta C, Choi KH. Biochemistry 51 5921-5931 (2012)
  2. Structural and functional analyses of a conserved hydrophobic pocket of flavivirus methyltransferase. Dong H, Liu L, Zou G, Zhao Y, Li Z, Lim SP, Shi PY, Li H. J. Biol. Chem. 285 32586-32595 (2010)
  3. Flavivirus RNA cap methyltransferase: structure, function, and inhibition. Liu L, Dong H, Chen H, Zhang J, Ling H, Li Z, Shi PY, Li H. Front Biol (Beijing) 5 286-303 (2010)
  4. The crystal structure of Zika virus NS5 reveals conserved drug targets. Duan W, Song H, Wang H, Chai Y, Su C, Qi J, Shi Y, Gao GF. EMBO J. 36 919-933 (2017)
  5. Refolding of a fully functional flavivirus methyltransferase revealed that S-adenosyl methionine but not S-adenosyl homocysteine is copurified with flavivirus methyltransferase. Brecher MB, Li Z, Zhang J, Chen H, Lin Q, Liu B, Li H. Protein Sci. 24 117-128 (2015)
  6. Sequence, structure and function relationships in flaviviruses as assessed by evolutive aspects of its conserved non-structural protein domains. da Fonseca NJ, Lima Afonso MQ, Pedersolli NG, de Oliveira LC, Andrade DS, Bleicher L. Biochem. Biophys. Res. Commun. 492 565-571 (2017)