3GCZ

Yokose virus Methyltransferase in complex with AdoMet

Summary for 3GCZ

• Entry DOI: 10.2210/pdb3gcz/pdb
• Descriptor: Polyprotein, S-ADENOSYLMETHIONINE, GLYCEROL, ... (5 entities in total)
• Functional Keywords: flavivirus, rna capping, methyltransferase, viral enzyme structure, atp-binding, nucleotide-binding, rna replication, structural genomics, structural proteomics in europe, spine, transferase
• Biological source: Yokose virus
• Cellular location: Envelope protein E: Virion membrane; Multi- pass membrane protein: Q7T918
• Total number of polymer chains: 1
• Total formula weight: 32607.30

Authors

Bollati, M.,Milani, M.,Mastrangelo, E.,Bolognesi, M.,Structural Proteomics in Europe (SPINE) (deposition date: 2009-02-23, release date: 2009-03-24, Last modification date: 2023-11-01)

Primary citation

Bollati, M.,Milani, M.,Mastrangelo, E.,de Lambellarie, X.,Canard, B.,Bolognesi, M.
Crystal structure of a methyltransferase from a no-known-vector Flavivirus
Biochem.Biophys.Res.Commun., 382:200-204, 2009

PubMed Abstract: 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.

PubMed: 19275894
DOI: 10.1016/j.bbrc.2009.03.008

Experimental method

X-RAY DIFFRACTION (1.7 Å)