1CY9

CRYSTAL STRUCTURE OF THE 30 KDA FRAGMENT OF E. COLI DNA TOPOISOMERASE I. MONOCLINIC FORM

Summary for 1CY9

• Entry DOI: 10.2210/pdb1cy9/pdb
• Related: 1CY0 1CY1 1CY2 1CY4 1CY6 1CY7 1CY8 1CYY
• Descriptor: DNA TOPOISOMERASE I (2 entities in total)
• Functional Keywords: dna topoisomerase, decatenating enzyme, isomerase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 59319.19

Authors

Feinberg, H.,Lima, C.,Mondragon, A. (deposition date: 1999-08-31, release date: 2000-03-08, Last modification date: 2024-02-07)

Primary citation

Feinberg, H.,Lima, C.D.,Mondragon, A.
Conformational changes in E. coli DNA topoisomerase I.
Nat.Struct.Biol., 6:918-922, 1999

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: 10504724
DOI: 10.1038/13283

Experimental method

X-RAY DIFFRACTION (1.8 Å)