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2KXE

N-terminal domain of the DP1 subunit of an archaeal D-family DNA polymerase

Summary for 2KXE
Entry DOI10.2210/pdb2kxe/pdb
NMR InformationBMRB: 16986
DescriptorDNA polymerase II small subunit (1 entity in total)
Functional Keywordsdna polymerase, d-family, small subunit, archara, helical bundle, transferase
Biological sourcePyrococcus horikoshii
Total number of polymer chains1
Total formula weight8534.80
Authors
Yamasaki, K.,Matsui, I. (deposition date: 2010-04-30, release date: 2010-08-18, Last modification date: 2024-05-15)
Primary citationYamasaki, 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: 20598295
DOI: 10.1016/j.febslet.2010.06.026
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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数据于2025-06-18公开中

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