Article ID Journal Published Year Pages File Type
2048156 FEBS Letters 2011 7 Pages PDF
Abstract

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 ∼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 ∼50 N-terminal residues with their own catalytic region (792–1163).Structured summaryDP2binds to DP2 by molecular sieving(View interaction)DP2binds to DP2 by fluorescence technology(View interaction)DP2binds to DP2 by circular dichroism(View interaction)

Related Topics
Life Sciences Agricultural and Biological Sciences Plant Science
Authors
, , , , ,