Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Hopfner, K.P. et al.

Hopfner, Eichinger, Engh, Laue, Ankenbauer, Huber, Angerer,

Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius.

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.[1]

References

Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius. Hopfner, K.P., Eichinger, A., Engh, R.A., Laue, F., Ankenbauer, W., Huber, R., Angerer, B. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]

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