3O59

DNA polymerase D large subunit DP2(1-300) from Pyrococcus horikoshii

Summary for 3O59

• Entry DOI: 10.2210/pdb3o59/pdb
• Descriptor: DNA polymerase II large subunit (2 entities in total)
• Functional Keywords: alpha helical structure, dna polymerase, transferase
• Biological source: Pyrococcus horikoshii
• Total number of polymer chains: 1
• Total formula weight: 33910.39

Authors

Yokoyama, H.,Shen, Y.,Matsui, I. (deposition date: 2010-07-28, release date: 2011-01-05, Last modification date: 2024-11-20)

Primary citation

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., 585:452-458, 2011

PubMed 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).

PubMed: 21192935
DOI: 10.1016/j.febslet.2010.12.040

Experimental method

X-RAY DIFFRACTION (2.2 Å)