6Q4V
KlenTaq DNA polymerase in complex with dATP
6Q4V の概要
| エントリーDOI | 10.2210/pdb6q4v/pdb |
| 分子名称 | DNA polymerase I, thermostable, DNA (5'-D(*GP*AP*CP*CP*AP*CP*GP*GP*CP*CP*AP*(DOC))-3'), DNA (5'-D(*AP*AP*CP*TP*GP*TP*GP*GP*CP*CP*GP*TP*GP*GP*TP*C)-3'), ... (8 entities in total) |
| 機能のキーワード | modified nucleotide klentaq dna polymerase next-generation sequencing, dna binding protein |
| 由来する生物種 | Thermus aquaticus 詳細 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 70232.21 |
| 構造登録者 | |
| 主引用文献 | Kropp, H.M.,Diederichs, K.,Marx, A. The Structure of an Archaeal B-Family DNA Polymerase in Complex with a Chemically Modified Nucleotide. Angew.Chem.Int.Ed.Engl., 58:5457-5461, 2019 Cited by PubMed Abstract: Archaeal B-family DNA polymerases (DNA pols) are the driving force of cutting-edge biotechnological applications like next-generation sequencing. The acceptance of chemically modified nucleotides by DNA pols is key to these technologies. Until now, no structural data have been available for these DNA pols in complex with modified substrates, which could build the basis for understanding interactions between the enzyme and the chemically modified nucleotide and for the further development of next-generation nucleotides. For the first time, we crystallized an exonuclease-deficient variant of the wild-type B-family KOD DNA pol with a modified nucleotide in a closed, ternary complex. We also crystalized the A-family DNA pol KlenTaq with the same nucleotide. The reported structural data reveal how the protein and the DNA modulate two distinct conformations of the appended moiety in the A- and B-family DNA pols and how these influence the processing of the modified nucleotide. Overall, this study provides first insight into the interplay between B-family DNA pols and relevant modified substrates. PubMed: 30761722DOI: 10.1002/anie.201900315 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.006 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






