1TGO

THERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUS

1TGO の概要

• エントリーDOI: 10.2210/pdb1tgo/pdb
• 分子名称: PROTEIN (THERMOSTABLE B DNA POLYMERASE) (2 entities in total)
• 機能のキーワード: dna polymerase, replication, disulfide bonds, transferase
• 由来する生物種: Thermococcus gorgonarius
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 89952.23

構造登録者

Hopfner, K.-P.,Eichinger, A.,Engh, R.A.,Laue, F.,Ankenbauer, W.,Huber, R.,Angerer, B. (登録日: 1999-02-23, 公開日: 1999-03-22, 最終更新日: 2024-11-20)

主引用文献

Hopfner, K.P.,Eichinger, A.,Engh, R.A.,Laue, F.,Ankenbauer, W.,Huber, R.,Angerer, B.
Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius.
Proc.Natl.Acad.Sci.USA, 96:3600-3605, 1999

PubMed Abstract: Most known archaeal DNA polymerases belong to the type B family, which also includes the DNA replication polymerases of eukaryotes, but maintain high fidelity at extreme conditions. We describe here the 2.5 A resolution crystal structure of a DNA polymerase from the Archaea Thermococcus gorgonarius and identify structural features of the fold and the active site that are likely responsible for its thermostable function. Comparison with the mesophilic B type DNA polymerase gp43 of the bacteriophage RB69 highlights thermophilic adaptations, which include the presence of two disulfide bonds and an enhanced electrostatic complementarity at the DNA-protein interface. In contrast to gp43, several loops in the exonuclease and thumb domains are more closely packed; this apparently blocks primer binding to the exonuclease active site. A physiological role of this "closed" conformation is unknown but may represent a polymerase mode, in contrast to an editing mode with an open exonuclease site. This archaeal B DNA polymerase structure provides a starting point for structure-based design of polymerases or ligands with applications in biotechnology and the development of antiviral or anticancer agents.

PubMed: 10097083
DOI: 10.1073/pnas.96.7.3600

実験手法

X-RAY DIFFRACTION (2.5 Å)