ユカリオットトポイソメラーゼIとサイト固有のリコンビネーゼとの間の構造とメカニズムの保存
C Cheng1, P Kussie, N Pavletich
1Molecular Biology Program, Sloan-Kettering Institute, New York, New York 10021, USA.
Cell
|April 7, 1998
まとめ
Vaccinia DNAトポイソメラーゼは,DNAを分解して再結合するために触媒ドメインを使用します. このドメインはこのドメインです.
科学分野:
- バイオケミストリー バイオケミストリー
- 分子生物学は分子生物学である.
- 構造生物学 構造生物学とは
背景:
- ワクチンDNAトポイソメラーゼは,DNAトポロジーを調節する酵素です.
- IB型トポイソメラーゼは,DNA操作に不可欠な,保存された触媒残基を共有しています.
研究 の 目的:
- Vaccinia DNA topoisomeraseの触媒領域を調査するために.
- トポイソメラーゼとサイト固有のリコンビネーゼの構造的,機能的関係を理解する.
主な方法:
- 触媒ドメインの3D構造を決定するX線結晶学 (Topo(81-314)).
- トポイソメラーゼ触媒ドメインとサイト固有のリコンビネーゼの比較構造分析.
主要な成果:
- C末端の触媒ドメイン (Topo ((81-314)) は,DNA鎖移転反応には十分である.
- 保存されたアミノ酸の触媒ペンタドは,DNAに対する核愛性の攻撃を容易にします.
- アルファヘリクとベータシートを特徴とする触媒ドメインの構造は,サイト固有の再結合と似ています.
結論:
- Vaccinia DNAトポイソメラーゼの触媒ドメインは,サイト固有のリコンビネーゼと構造的ホモロジーを共有しています.
- 保存された三次構造は,祖先の鎖移転酵素としてこれらの酵素の共通の進化的起源を示唆しています.
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