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== Function == | == 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). | [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). | ||
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== 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> | |||
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==See Also== | ==See Also== | ||
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]] | *[[DNA polymerase 3D structures|DNA polymerase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 05:12, 21 November 2024
DNA polymerase D large subunit DP2(1-300) from Pyrococcus horikoshiiDNA polymerase D large subunit DP2(1-300) from Pyrococcus horikoshii
Structural highlights
FunctionDP2L_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). Publication Abstract from PubMedArchaea-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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