Download MendeleyThe 1.85 A structure of vaccinia protein VP39: a bifunctional enzyme that participates in the modification of both mRNA ends.
Hodel, A.E., Gershon, P.D., Shi, X., Quiocho, F.A.(1996) Cell 85: 247-256
- PubMed: 8612277
- DOI: https://doi.org/10.1016/s0092-8674(00)81101-0
- Primary Citation of Related Structures:
1VPT - PubMed Abstract:
VP39 is a bifunctional vaccinia virus protein that acts as both an mRNA cap-specific RNA 2'-O-methyltransferase and a poly(A) polymerase processivity factor. Here, we report the 1.85 A crystal structure of a VP39 variant complexed with its AdoMet cofactor. VP39 comprises a single core domain with structural similarity to the catalytic domains of other methyltransferases. Surface features and mutagenesis data suggest two possible RNA-binding sites with novel underlying architecture, one of which forms a cleft spanning the region adjacent to the methyltransferase active site. This report provides a prototypic structure for an RNA methyltransferase, a protein that interacts with the mRNA 5' cap, and an intact poxvirus protein.
Organizational Affiliation:
Howard Hughes Medical Institute, Baylor College of Medicine, Houston, Texas 77030, USA.
