1A41

TYPE 1-TOPOISOMERASE CATALYTIC FRAGMENT FROM VACCINIA VIRUS

1A41 の概要

• エントリーDOI: 10.2210/pdb1a41/pdb
• 分子名称: TOPOISOMERASE I, SULFATE ION (3 entities in total)
• 機能のキーワード: type 1b topoisomerase, isomerase
• 由来する生物種: Vaccinia virus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27371.02

構造登録者

Cheng, C.,Kussie, P.,Pavletich, N.,Shuman, S. (登録日: 1998-02-10, 公開日: 1999-06-01, 最終更新日: 2024-02-07)

主引用文献

Cheng, C.,Kussie, P.,Pavletich, N.,Shuman, S.
Conservation of structure and mechanism between eukaryotic topoisomerase I and site-specific recombinases.
Cell(Cambridge,Mass.), 92:841-850, 1998

PubMed Abstract: Vaccinia DNA topoisomerase breaks and rejoins DNA strands through a DNA-(3'-phosphotyrosyl)-enzyme intermediate. A C-terminal catalytic domain, Topo(81-314), suffices for transesterification chemistry. The domain contains a constellation of five amino acids, conserved in all eukaryotic type IB topoisomerases, that catalyzes attack of the tyrosine nucleophile on the scissile phosphate. The structure of the catalytic domain, consisting of ten alpha helices and a three-strand beta sheet, resembles the catalytic domains of site-specific recombinases that act via a topoisomerase IB-like mechanism. The topoisomerase catalytic pentad is conserved in the tertiary structures of the recombinases despite scant sequence similarity overall. This implies that the catalytic domains of type IB topoisomerases and recombinases derive from a common ancestral strand transferase.

PubMed: 9529259
DOI: 10.1016/S0092-8674(00)81411-7

実験手法

X-RAY DIFFRACTION (2.3 Å)