1KTQ

DNA POLYMERASE

Summary for 1KTQ

• Entry DOI: 10.2210/pdb1ktq/pdb
• Descriptor: DNA POLYMERASE I (2 entities in total)
• Functional Keywords: nucleotidyltransferase, dna-replication
• Biological source: Thermus aquaticus
• Total number of polymer chains: 1
• Total formula weight: 61250.34

Authors

Korolev, S.,Waksman, G. (deposition date: 1995-08-16, release date: 1996-11-08, Last modification date: 2024-02-14)

Primary citation

Korolev, S.,Nayal, M.,Barnes, W.M.,Di Cera, E.,Waksman, G.
Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5-A resolution: structural basis for thermostability.
Proc.Natl.Acad.Sci.USA, 92:9264-9268, 1995

PubMed 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.

PubMed: 7568114
DOI: 10.1073/pnas.92.20.9264

Experimental method

X-RAY DIFFRACTION (2.5 Å)