3OWG

Crystal structure of vaccinia virus Polyadenylate polymerase(vp55)

Summary for 3OWG

• Entry DOI: 10.2210/pdb3owg/pdb
• Related: 2GA9 3ER8 3ER9 3ERC
• Descriptor: Poly(A) polymerase catalytic subunit (1 entity in total)
• Functional Keywords: rna polyadenylate polymerase complex, translocation, polyadenylate polymerase, transferase
• Biological source: Vaccinia virus WR (VACV)
• Total number of polymer chains: 2
• Total formula weight: 112806.01

Authors

Li, C.,Li, H.,Zhou, S.,Gershon, P.D.,Poulos, T.L. (deposition date: 2010-09-17, release date: 2011-09-21, Last modification date: 2023-09-06)

Primary citation

Li, H.,Li, C.,Zhou, S.,Poulos, T.L.,Gershon, P.D.
Domain-level rocking motion within a polymerase that translocates on single-stranded nucleic acid.
Acta Crystallogr.,Sect.D, 69:617-624, 2013

PubMed Abstract: Vaccinia virus poly(A) polymerase (VP55) is the only known polymerase that can translocate independently with respect to single-stranded nucleic acid (ssNA). Previously, its structure has only been solved in the context of the VP39 processivity factor. Here, a crystal structure of unliganded monomeric VP55 has been solved to 2.86 Å resolution, showing the first backbone structural isoforms among either VP55 or its processivity factor (VP39). Backbone differences between the two molecules of VP55 in the asymmetric unit indicated that unliganded monomeric VP55 can undergo a `rocking' motion of the N-terminal domain with respect to the other two domains, which may be `rigidified' upon VP39 docking. This observation is consistent with previously demonstrated experimental molecular dynamics of the monomer during translocation with respect to nucleic acid and with different mechanisms of translocation in the presence and absence of processivity factor VP39. Side-chain conformational changes in the absence of ligand were observed at a key primer contact site and at the catalytic center of VP55. The current structure completes the trio of possible structural forms for VP55 and VP39, namely the VP39 monomer, the VP39-VP55 heterodimer and the VP55 monomer.

PubMed: 23519670
DOI: 10.1107/S0907444913000346

Experimental method

X-RAY DIFFRACTION (2.86 Å)