Conformational changes in E. coli DNA topoisomerase I

H. Feinberg; C. D. Lima; A. Mondragon

doi:10.1038/13283

Conformational changes in E. coli DNA topoisomerase I

H. Feinberg, C. D. Lima, A. Mondragon^*

^*Corresponding author for this work

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

46 Scopus citations

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.

Original language	English (US)
Pages (from-to)	918-922
Number of pages	5
Journal	Nature Structural Biology
Volume	6
Issue number	10
DOIs	https://doi.org/10.1038/13283
State	Published - 1999

Funding

Use of the Advanced Photon Source was supported by the DOE. We thank past and present members of the laboratory and A. Changela, R. DiGate, L. Godley, M. Gwynn, T. Jardetzky, K. Perry, X. Qiu, A. Rosenzweig, A. Tackle, J. Widom and X. Yang, for help, comments and suggestions. We thank BNLS, CHESS, DND-CAT, ELETTRA and SSRL for access to their beamlines and help during data collection. We thank M. Blum of MAR USA for the use of the MAR CCD detector for experiments at BNLS. This work was supported by the NIH and by SmithKline Beecham Pharmaceuticals. Portions of this work were performed at the DuPont-Northwestern-Dow Collaborative Access Team (DND-CAT) Synchrotron Research Center at the Advanced Photon Source. DND-CAT is supported by DuPont, Dow, NSF and the State of Illinois.

ASJC Scopus subject areas

Structural Biology
Biochemistry
Genetics

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10.1038/13283

Cite this

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title = "Conformational changes in E. coli DNA topoisomerase I",

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.",

author = "H. Feinberg and Lima, {C. D.} and A. Mondragon",

note = "Funding Information: Use of the Advanced Photon Source was supported by the DOE. Funding Information: We thank past and present members of the laboratory and A. Changela, R. DiGate, L. Godley, M. Gwynn, T. Jardetzky, K. Perry, X. Qiu, A. Rosenzweig, A. Tackle, J. Widom and X. Yang, for help, comments and suggestions. We thank BNLS, CHESS, DND-CAT, ELETTRA and SSRL for access to their beamlines and help during data collection. We thank M. Blum of MAR USA for the use of the MAR CCD detector for experiments at BNLS. This work was supported by the NIH and by SmithKline Beecham Pharmaceuticals. Portions of this work were performed at the DuPont-Northwestern-Dow Collaborative Access Team (DND-CAT) Synchrotron Research Center at the Advanced Photon Source. DND-CAT is supported by DuPont, Dow, NSF and the State of Illinois.",

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Conformational changes in E. coli DNA topoisomerase I

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

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

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Conformational changes in E. coli DNA topoisomerase I

Abstract

Funding

ASJC Scopus subject areas

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

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

Cite this