Structural highlights
Function
[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).
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Matsui I, Urushibata Y, Shen Y, Matsui E, Yokoyama H. 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. FEBS Lett. 2011 Feb 4;585(3):452-8. Epub 2010 Dec 28. PMID:21192935 doi:10.1016/j.febslet.2010.12.040
