View source for 4gfj


==Crystal structure of Topo-78, an N-terminal 78kDa fragment of topoisomerase V==
<StructureSection load='4gfj' size='340' side='right'caption='[[4gfj]], [[Resolution|resolution]] 2.91&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4gfj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanopyrus_kandleri_AV19 Methanopyrus kandleri AV19]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GFJ 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]] 2.91&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4gfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gfj OCA], [https://pdbe.org/4gfj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gfj RCSB], [https://www.ebi.ac.uk/pdbsum/4gfj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gfj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F1SVL0_METKA F1SVL0_METKA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Topoisomerase V (Topo-V) is the only member of a novel topoisomerase subtype. Topo-V is unique because it is a bifunctional enzyme carrying both topoisomerase and DNA repair lyase activities within the same protein. Previous studies had shown that the topoisomerase domain spans the N-terminus of the protein and is followed by 12 tandem helix-hairpin-helix [(HhH)(2)] domains. There are at least two DNA repair lyase active sites for apurinic/apyrimidinic (AP) site processing, one within the N-terminal region and the second within the C-terminal domain of Topo-V, but their exact locations and characteristics are unknown. In the present study, the N-terminal 78-kDa fragment of Topo-V (Topo-78), containing the topoisomerase domain and one of the lyase DNA repair domains, was characterized by structural and biochemical studies. The results show that an N-terminal 69-kDa fragment is the minimal fragment with both topoisomerase and AP lyase activities. The lyase active site of Topo-78 is at the junction of the fifth and sixth (HhH)(2) domains. From the biochemical and structural data, it appears that Lys571 is the most probable nucleophile responsible for the lyase activity. Our experiments also suggest that Topo-V most likely acts as a Class I AP endonuclease in vivo.

Identification of one of the apurinic/apyrimidinic lyase active sites of topoisomerase V by structural and functional studies.,Rajan R, Prasad R, Taneja B, Wilson SH, Mondragon A Nucleic Acids Res. 2012 Nov 3. PMID:23125368<ref>PMID:23125368</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4gfj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Topoisomerase 3D structures|Topoisomerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanopyrus kandleri AV19]]
[[Category: Mondragon A]]
[[Category: Prasad R]]
[[Category: Rajan R]]
[[Category: Taneja B]]
[[Category: Wilson SH]]