View source for 3owg


==Crystal structure of vaccinia virus Polyadenylate polymerase(vp55)==
<StructureSection load='3owg' size='340' side='right'caption='[[3owg]], [[Resolution|resolution]] 2.86&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3owg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus_WR Vaccinia virus WR]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OWG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.86&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3owg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3owg OCA], [https://pdbe.org/3owg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3owg RCSB], [https://www.ebi.ac.uk/pdbsum/3owg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3owg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PAP1_VACCW PAP1_VACCW] Polymerase that creates the 3'-poly(A) tail of mRNA's.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 A 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.

Domain-level rocking motion within a polymerase that translocates on single-stranded nucleic acid.,Li H, Li C, Zhou S, Poulos TL, Gershon PD Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):617-24. doi:, 10.1107/S0907444913000346. Epub 2013 Mar 14. PMID:23519670<ref>PMID:23519670</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3owg" style="background-color:#fffaf0;"></div>

==See Also==
*[[Poly(A) polymerase 3D structures|Poly(A) polymerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vaccinia virus WR]]
[[Category: Gershon PD]]
[[Category: Li C]]
[[Category: Li H]]
[[Category: Poulos TL]]
[[Category: Zhou S]]