2KXE
N-terminal domain of the DP1 subunit of an archaeal D-family DNA polymerase
Summary for 2KXE
Entry DOI | 10.2210/pdb2kxe/pdb |
NMR Information | BMRB: 16986 |
Descriptor | DNA polymerase II small subunit (1 entity in total) |
Functional Keywords | dna polymerase, d-family, small subunit, archara, helical bundle, transferase |
Biological source | Pyrococcus horikoshii |
Total number of polymer chains | 1 |
Total formula weight | 8534.80 |
Authors | Yamasaki, K.,Matsui, I. (deposition date: 2010-04-30, release date: 2010-08-18, Last modification date: 2024-05-15) |
Primary citation | Yamasaki, K.,Urushibata, Y.,Yamasaki, T.,Arisaka, F.,Matsui, I. Solution structure of the N-terminal domain of the archaeal D-family DNA polymerase small subunit reveals evolutionary relationship to eukaryotic B-family polymerases Febs Lett., 584:3370-3375, 2010 Cited by PubMed Abstract: Archaea-specific D-family DNA polymerase forms a heterotetramer consisting of two large polymerase subunits and two small exonuclease subunits. We analyzed the structure of the N-terminal 200 amino-acid regulatory region of the small subunit by NMR and revealed that the N-terminal approximately 70 amino-acid region is folded. The structure consists of a four-alpha-helix bundle including a short parallel beta-sheet, which is similar to the N-terminal regions of the B subunits of human DNA polymerases alpha and epsilon, establishing evolutionary relationships among these archaeal and eukaryotic polymerases. We observed monomer-dimer equilibrium of this domain, which may be related to holoenzyme architecture and/or functional regulation. PubMed: 20598295DOI: 10.1016/j.febslet.2010.06.026 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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