4KTQ

BINARY COMPLEX OF THE LARGE FRAGMENT OF DNA POLYMERASE I FROM T. AQUATICUS BOUND TO A PRIMER/TEMPLATE DNA

4KTQ の概要

• エントリーDOI: 10.2210/pdb4ktq/pdb
• 分子名称: DNA (5'-D(*GP*AP*CP*CP*AP*CP*GP*GP*CP*GP*CP*(DOC))-3'), DNA (5'-D(*GP*GP*GP*CP*GP*CP*CP*GP*TP*GP*GP*TP*C)-3'), PROTEIN (LARGE FRAGMENT OF DNA POLYMERASE I), ... (4 entities in total)
• 機能のキーワード: large fragement of taq dna polymerase i, protein/dna, transferase-dna complex, transferase/dna
• 由来する生物種: Thermus aquaticus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 68507.85

構造登録者

Li, Y.,Waksman, G. (登録日: 1998-09-09, 公開日: 1999-01-13, 最終更新日: 2024-02-28)

主引用文献

Li, Y.,Korolev, S.,Waksman, G.
Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide incorporation.
EMBO J., 17:7514-7525, 1998

PubMed Abstract: The crystal structures of two ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I (Klentaq1) with a primer/template DNA and dideoxycytidine triphosphate, and that of a binary complex of the same enzyme with a primer/template DNA, were determined to a resolution of 2.3, 2.3 and 2.5 A, respectively. One ternary complex structure differs markedly from the two other structures by a large reorientation of the tip of the fingers domain. This structure, designated 'closed', represents the ternary polymerase complex caught in the act of incorporating a nucleotide. In the two other structures, the tip of the fingers domain is rotated outward by 46 degrees ('open') in an orientation similar to that of the apo form of Klentaq1. These structures provide the first direct evidence in DNA polymerase I enzymes of a large conformational change responsible for assembling an active ternary complex.

PubMed: 9857206
DOI: 10.1093/emboj/17.24.7514

実験手法

X-RAY DIFFRACTION (2.5 Å)