View source for 3o59


==DNA polymerase D large subunit DP2(1-300) from Pyrococcus horikoshii==
<StructureSection load='3o59' size='340' side='right'caption='[[3o59]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3o59]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O59 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3o59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o59 OCA], [https://pdbe.org/3o59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o59 RCSB], [https://www.ebi.ac.uk/pdbsum/3o59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o59 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DP2L_PYRHO DP2L_PYRHO] Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Archaea-specific D-family DNA polymerase forms a heterotetramer consisting of two large polymerase subunits and two small exonuclease subunits. The N-terminal (1-300) domain structure of the large subunit was determined by X-ray crystallography, although approximately 50 N-terminal residues were disordered. The determined structure consists of nine alpha helices and three beta strands. We also identified the DNA-binding ability of the domain by SPR measurement. The N-terminal (1-100) region plays crucial roles in the folding of the large subunit dimer by connecting the approximately 50 N-terminal residues with their own catalytic region (792-1163). STRUCTURED SUMMARY: DP2binds to DP2 by molecular sieving(View interaction) DP2binds to DP2 by fluorescence technology(View interaction) DP2binds to DP2 by circular dichroism(View interaction).

Novel structure of an N-terminal domain that is crucial for the dimeric assembly and DNA-binding of an archaeal DNA polymerase D large subunit from Pyrococcus horikoshii.,Matsui I, Urushibata Y, Shen Y, Matsui E, Yokoyama H FEBS Lett. 2011 Feb 4;585(3):452-8. Epub 2010 Dec 28. PMID:21192935<ref>PMID:21192935</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3o59" style="background-color:#fffaf0;"></div>

==See Also==
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus horikoshii]]
[[Category: Matsui I]]
[[Category: Shen Y]]
[[Category: Yokoyama H]]