1CY4

COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 5'pTpTpTp3'

1CY4 の概要

• エントリーDOI: 10.2210/pdb1cy4/pdb
• 関連するPDBエントリー: 1CY0 1CY1 1CY2 1CY6 1CY7 1CY8 1CY9 1CYY
• 分子名称: DNA TOPOISOMERASE I, PHOSPHATE ION, THYMIDINE-5'-PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: dna topoisomerase, relaxing enzyme, isomerase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 68149.62

構造登録者

Feinberg, H.,Changela, A.,Mondragon, A. (登録日: 1999-08-31, 公開日: 2000-03-08, 最終更新日: 2024-05-22)

主引用文献

Feinberg, H.,Changela, A.,Mondragon, A.
Protein-nucleotide interactions in E. coli DNA topoisomerase I.
Nat.Struct.Biol., 6:961-968, 1999

PubMed Abstract: DNA topoisomerases are the enzymes responsible for controlling and maintaining the topological states of DNA. Type IA enzymes work by transiently breaking the phosphodiester backbone of one strand to allow passage of another strand through the break. The protein has to perform complex rearrangements of the DNA, and hence it is likely that different regions of the enzyme bind DNA with different affinities. In order to identify some of the DNA binding sites in the protein, we have solved the structures of several complexes of the 67 kDa N-terminal fragment of Escherichia coli DNA topoisomerase I with mono- and trinucleotides. There are five different binding sites in the complexes, one of which is adjacent to the active site. Two other sites are in the central hole of the protein and may represent general DNA binding regions. The positions of these sites allow us to identify different DNA binding regions and to understand their possible roles in the catalytic cycle.

PubMed: 10504732
DOI: 10.1038/13333

実験手法

X-RAY DIFFRACTION (2.55 Å)