1TGO

THERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUS

Summary for 1TGO

• Entry DOI: 10.2210/pdb1tgo/pdb
• Descriptor: PROTEIN (THERMOSTABLE B DNA POLYMERASE) (2 entities in total)
• Functional Keywords: dna polymerase, replication, disulfide bonds, transferase
• Biological source: Thermococcus gorgonarius
• Total number of polymer chains: 1
• Total formula weight: 89952.23

Authors

Hopfner, K.-P.,Eichinger, A.,Engh, R.A.,Laue, F.,Ankenbauer, W.,Huber, R.,Angerer, B. (deposition date: 1999-02-23, release date: 1999-03-22, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)