1VPT

AS11 VARIANT OF VACCINIA VIRUS PROTEIN VP39 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE

Summary for 1VPT

• Entry DOI: 10.2210/pdb1vpt/pdb
• Descriptor: VP39, S-ADENOSYLMETHIONINE (3 entities in total)
• Functional Keywords: rna cap, poly(a) polymerase, vaccinia, methyltransferase
• Biological source: Vaccinia virus
• Total number of polymer chains: 1
• Total formula weight: 40324.33

Authors

Hodel, A.E.,Gershon, P.D.,Shi, X.,Quiocho, F.A. (deposition date: 1996-03-20, release date: 1996-08-17, Last modification date: 2024-02-14)

Primary citation

Hodel, A.E.,Gershon, P.D.,Shi, X.,Quiocho, F.A.
The 1.85 A structure of vaccinia protein VP39: a bifunctional enzyme that participates in the modification of both mRNA ends.
Cell(Cambridge,Mass.), 85:247-256, 1996

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.

PubMed: 8612277
DOI: 10.1016/S0092-8674(00)81101-0

Experimental method

X-RAY DIFFRACTION (1.8 Å)