Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5-A resolution: structural basis for thermostability.
- 26 September 1995
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 92 (20) , 9264-9268
- https://doi.org/10.1073/pnas.92.20.9264
Abstract
The crystal structure of the large fragment of the Thermus aquaticus DNA polymerase (Klentaq1), determined at 2.5-A resolution, demonstrates a compact two-domain architecture. The C-terminal domain is identical in fold to the equivalent region of the Klenow fragment of Escherichia coli DNA polymerase I (Klenow pol I). Although the N-terminal domain of Klentaq1 differs greatly in sequence from its counterpart in Klenow pol I, it has clearly evolved from a common ancestor. The structure of Klentaq1 reveals the strategy utilized by this protein to maintain activity at high temperatures and provides the structural basis for future improvements of the enzyme.Keywords
This publication has 35 references indexed in Scilit:
- Crystal Structure of Rat DNA Polymerase β: Evidence for a Common Polymerase MechanismScience, 1994
- Crystal structure of bacteriophage T7 RNA polymerase at 3.3 Å resolutionNature, 1993
- High-fidelity amplification using a thermostable DNA polymerase isolated from Pyrococcus furiosusGene, 1991
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991
- Current approaches to macromolecular crystallizationEuropean Journal of Biochemistry, 1990
- Engineering protein thermal stability: Sequence statistics point to residue substitutions in α-helicesJournal of Molecular Biology, 1989
- Primer-Directed Enzymatic Amplification of DNA with a Thermostable DNA PolymeraseScience, 1988
- Amino‐aromatic interactions in proteinsFEBS Letters, 1986
- Enzymatic Amplification of β-Globin Genomic Sequences and Restriction Site Analysis for Diagnosis of Sickle Cell AnemiaScience, 1985
- Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMPNature, 1985