3o59
From Proteopedia
(Difference between revisions)
(6 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | [[Image:3o59.png|left|200px]] | ||
- | + | ==DNA polymerase D large subunit DP2(1-300) from Pyrococcus horikoshii== | |
+ | <StructureSection load='3o59' size='340' side='right'caption='[[3o59]], [[Resolution|resolution]] 2.20Å' 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]] 2.2Å</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 3o59" style="background-color:#fffaf0;"></div> | |
- | + | ||
==See Also== | ==See Also== | ||
- | *[[DNA polymerase|DNA polymerase]] | + | *[[DNA polymerase 3D structures|DNA polymerase 3D structures]] |
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
- | [[Category: | + | </StructureSection> |
+ | [[Category: Large Structures]] | ||
[[Category: Pyrococcus horikoshii]] | [[Category: Pyrococcus horikoshii]] | ||
- | [[Category: Matsui | + | [[Category: Matsui I]] |
- | [[Category: Shen | + | [[Category: Shen Y]] |
- | [[Category: Yokoyama | + | [[Category: Yokoyama H]] |
- | + | ||
- | + | ||
- | + |
Current revision
DNA polymerase D large subunit DP2(1-300) from Pyrococcus horikoshii
|