5VU5

TNA polymerase, apo

5VU5 の概要

• エントリーDOI: 10.2210/pdb5vu5/pdb
• 関連するPDBエントリー: 5VU6 5VU7 5VU8 5VU9
• 分子名称: DNA polymerase (1 entity in total)
• 機能のキーワード: protein-nucleic acid complex, transferase
• 由来する生物種: Thermococcus kodakarensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 90130.62

構造登録者

Chim, N.,Chaput, J.C. (登録日: 2017-05-18, 公開日: 2017-12-06, 最終更新日: 2024-11-06)

主引用文献

Chim, N.,Shi, C.,Sau, S.P.,Nikoomanzar, A.,Chaput, J.C.
Structural basis for TNA synthesis by an engineered TNA polymerase.
Nat Commun, 8:1810-1810, 2017

PubMed Abstract: Darwinian evolution experiments carried out on xeno-nucleic acid (XNA) polymers require engineered polymerases that can faithfully and efficiently copy genetic information back and forth between DNA and XNA. However, current XNA polymerases function with inferior activity relative to their natural counterparts. Here, we report five X-ray crystal structures that illustrate the pathway by which α-(L)-threofuranosyl nucleic acid (TNA) triphosphates are selected and extended in a template-dependent manner using a laboratory-evolved polymerase known as Kod-RI. Structural comparison of the apo, binary, open and closed ternary, and translocated product detail an ensemble of interactions and conformational changes required to promote TNA synthesis. Close inspection of the active site in the closed ternary structure reveals a sub-optimal binding geometry that explains the slow rate of catalysis. This key piece of information, which is missing for all naturally occurring archaeal DNA polymerases, provides a framework for engineering new TNA polymerase variants.

PubMed: 29180809
DOI: 10.1038/s41467-017-02014-0

実験手法

X-RAY DIFFRACTION (2.8 Å)