5OMF

Closed, ternary structure of KOD DNA polymerase

5OMF の概要

• エントリーDOI: 10.2210/pdb5omf/pdb
• 分子名称: DNA polymerase,DNA polymerase,DNA polymerase, DNA (5'-D(P*CP*TP*GP*TP*GP*GP*CP*CP*GP*TP*GP*GP*TP*C)-3'), DNA (5'-D(*GP*AP*CP*CP*AP*CP*GP*GP*CP*CP*AP*C)-3'), ... (9 entities in total)
• 機能のキーワード: dna replication dna polymerase archaea, dna binding protein
• 由来する生物種: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 101008.74

構造登録者

Kropp, H.M.,Betz, K.,Wirth, J.,Diederichs, K.,Marx, A. (登録日: 2017-07-31, 公開日: 2017-12-20, 最終更新日: 2024-11-13)

主引用文献

Kropp, H.M.,Betz, K.,Wirth, J.,Diederichs, K.,Marx, A.
Crystal structures of ternary complexes of archaeal B-family DNA polymerases.
PLoS ONE, 12:e0188005-e0188005, 2017

PubMed Abstract: Archaeal B-family polymerases drive biotechnology by accepting a wide substrate range of chemically modified nucleotides. By now no structural data for archaeal B-family DNA polymerases in a closed, ternary complex are available, which would be the basis for developing next generation nucleotides. We present the ternary crystal structures of KOD and 9°N DNA polymerases complexed with DNA and the incoming dATP. The structures reveal a third metal ion in the active site, which was so far only observed for the eukaryotic B-family DNA polymerase δ and no other B-family DNA polymerase. The structures reveal a wide inner channel and numerous interactions with the template strand that provide space for modifications within the enzyme and may account for the high processivity, respectively. The crystal structures provide insights into the superiority over other DNA polymerases concerning the acceptance of modified nucleotides.

PubMed: 29211756
DOI: 10.1371/journal.pone.0188005

実験手法

X-RAY DIFFRACTION (2.092 Å)