1CYY
CRYSTAL STRUCTURE OF THE 30 KDA FRAGMENT OF E. COLI DNA TOPOISOMERASE I. HEXAGONAL FORM
1CYY の概要
| エントリーDOI | 10.2210/pdb1cyy/pdb |
| 関連するPDBエントリー | 1CY0 1CY1 1CY2 1CY4 1CY6 1CY7 1CY8 1CY9 |
| 分子名称 | DNA TOPOISOMERASE I, ZINC ION (3 entities in total) |
| 機能のキーワード | dna topoisomerase, decatenating enzyme, isomerase |
| 由来する生物種 | Escherichia coli |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 59384.60 |
| 構造登録者 | |
| 主引用文献 | Feinberg, H.,Lima, C.D.,Mondragon, A. Conformational changes in E. coli DNA topoisomerase I. Nat.Struct.Biol., 6:918-922, 1999 Cited by PubMed Abstract: DNA topoisomerases are the enzymes responsible for maintaining the topological states of DNA. In order to change the topology of DNA, topoisomerases pass one or two DNA strands through transient single or double strand breaks in the DNA phosphodiester backbone. It has been proposed that both type IA and type II enzymes change conformation dramatically during the reaction cycle in order to accomplish these transformations. In the case of Escherichia coli DNA topoisomerase I, it has been suggested that a 30 kDa fragment moves away from the rest of the protein to create an entrance into the central hole in the protein. Structures of the 30 kDa fragment reveal that indeed this fragment can change conformation significantly. The fragment is composed of two domains, and while the domains themselves remain largely unchanged, their relative arrangement can change dramatically. PubMed: 10504724DOI: 10.1038/13283 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.15 Å) |
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