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1TAU

TAQ POLYMERASE (E.C.2.7.7.7)/DNA/B-OCTYLGLUCOSIDE COMPLEX

1TAU の概要
エントリーDOI10.2210/pdb1tau/pdb
分子名称DNA (5'-D(*GP*CP*GP*AP*TP*CP*CP*G)-3'), DNA (5'-D(*CP*GP*GP*AP*TP*CP*GP*C)-3'), PROTEIN (TAQ POLYMERASE), ... (5 entities in total)
機能のキーワードprotein-dna complex, taq dna polymerase, 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99259.27
構造登録者
Eom, S.H.,Wang, J.,Steitz, T.A. (登録日: 1996-06-17, 公開日: 1997-04-18, 最終更新日: 2024-02-14)
主引用文献Eom, S.H.,Wang, J.,Steitz, T.A.
Structure of Taq ploymerase with DNA at the polymerase active site.
Nature, 382:278-281, 1996
Cited by
PubMed Abstract: The DNA polymerase from Thermus aquaticus (Taq polymerase) is homologous to Escherichia coli DNA polymerase I (Pol I) and likewise has domains responsible for DNA polymerase and 5' nuclease activities. The structures to the polymerase domains of Taq polymerase and of the Klenow fragment (KF) of Pol I are almost identical, whereas the structure of a vestigial editing 3'-5' exonuclease domain of Taq polymerase that lies between the other two domains is dramatically altered, resulting in the absence of this activity in the thermostable enzyme. The structures have been solved for editing complexes between KF and single-stranded DNA and for duplex DNA with a 3' overhanging single strand, but not for a complex containing duplex DNA at the polymerase active-site. Here we present the co-crystal structure of Taq polymerase with a blunt-ended duplex DNA bound to the polymerase active-site cleft; the DNA neither bends nor goes through the large polymerase cleft, and the structural form of the bound DNA is between the B and A forms. A wide minor groove allows access to protein side chains that hydrogen-bond to the N3 of purines and the O2 of pyrimidines at the blunt-end terminus. Part of the DNA bound to the polymerase site shares a common binding site with DNA bound to the exonuclease site, but they are translated relative to each other by several angstroms along their helix axes.
PubMed: 8717047
DOI: 10.1038/382278a0
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3 Å)
構造検証レポート
Validation report summary of 1tau
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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