3ERC

Crystal structure of the heterodimeric vaccinia virus mRNA polyadenylate polymerase with three fragments of RNA and 3'-deoxy ATP

Summary for 3ERC

• Entry DOI: 10.2210/pdb3erc/pdb
• Related: 2GA9 3ER8 3ER9
• Descriptor: Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase, Poly(A) polymerase catalytic subunit, RNA/DNA chimera (5'-D(CP*)R(UP*UP*)D(CP*C)-3'), ... (9 entities in total)
• Functional Keywords: polyadenylate polymerase, translocation, single tranded rna poly(a) polymerase, rna protein complex, processivity, heterodimer, nucleotidyltransferase, poxvirus; methyltransferase, mrna capping, mrna processing, s-adenosyl-l-methionine, transcription, transferase, transferase/dna, rna complex, transferase-dna, rna
• Biological source: vaccinia virus WR; More
• Cellular location: Virion : P07617
• Total number of polymer chains: 8
• Total formula weight: 187567.71

Authors

Li, C.,Li, H.,Zhou, S.,Poulos, T.L.,Gershon, P.D. (deposition date: 2008-10-01, release date: 2009-06-16, Last modification date: 2024-10-16)

Primary citation

Li, C.,Li, H.,Zhou, S.,Sun, E.,Yoshizawa, J.,Poulos, T.L.,Gershon, P.D.
Polymerase Translocation with Respect to Single-Stranded Nucleic Acid: Looping or Wrapping of Primer around a Poly(A) Polymerase
Structure, 17:680-689, 2009

PubMed Abstract: Vaccinia virus protein VP55 translocates continuously with respect to single-stranded nucleic acid while extending its 3'end. Here, all key sites of polymerase-primer interaction were identified, demonstrating the wrapping or looping of polyadenylation primer around the polymerase during translocation. Side-chain substitutions at one of the sites indicated its requirement for tail extension beyond approximately 12 nucleotides in length, and conformational changes observed upon oligonucleotide binding suggested allosteric connectivity during translocation. Conformational changes in VP39 upon VP55 binding suggested that, within the VP55-VP39 complex, VP39's mRNA 5' cap binding site closes. The crystallographic structure showed a PAPase catalytic center without side-chain substitutions, possessing two metal ions and with all known reactive and catalytic groups represented, fitting a classical two-metal ion mechanism for phosphoryl transfer.

PubMed: 19446524
DOI: 10.1016/j.str.2009.03.012

Experimental method

X-RAY DIFFRACTION (3.21 Å)