InterPro : IPR003601

Name  DNA topoisomerase, type IA, domain 2 Short Name  Topo_IA_2
Type  Domain Description  DNA topoisomerases regulate the number of topological links between two DNA strands (i.e. change the number of superhelical turns) by catalysing transient single- or double-strand breaks, crossing the strands through one another, then resealing the breaks []. These enzymes have several functions: to remove DNA supercoils during transcription and DNA replication; for strand breakage during recombination; for chromosome condensation; and to disentangle intertwined DNA during mitosis [, ]. DNA topoisomerases are divided into two classes: type I enzymes (; topoisomerases I, III and V) break single-strand DNA, and type II enzymes (; topoisomerases II, IV and VI) break double-strand DNA [].Type I topoisomerases are ATP-independent enzymes (except for reverse gyrase), and can be subdivided according to their structure and reaction mechanisms: type IA (bacterial and archaeal topoisomerase I, topoisomerase III and reverse gyrase) and type IB (eukaryotic topoisomerase I and topoisomerase V). These enzymes are primarily responsible for relaxing positively and/or negatively supercoiled DNA, except for reverse gyrase, which can introduce positive supercoils into DNA. This entry describes domain 2 found in type IA topoisomerases, which may be an extension of the Toprim domain. The structures of bacterial topoisomerases I and III have been shown to consist of four domains that together form a toroidal structure with a central hole large enough to accommodate single- and double-stranded DNA. The N-terminal Toprim domain together with domain 3 forms the active site of the enzyme, while domains 2 and 4 form a single-strand DNA-binding groove [, ]. The Toprim domain () forms a compact Rossmann fold that coordinates the Mg+2 ion [].
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

7 Found In

Id Name Short Name Type
IPR000380 DNA topoisomerase, type IA Topo_IA Family
IPR013497 DNA topoisomerase, type IA, central Topo_IA_cen Domain
IPR013824 DNA topoisomerase, type IA, central region, subdomain 1 Topo_IA_cen_sub1 Domain
IPR005733 DNA topoisomerase I, bacterial-type TopoI_bac-type Family
IPR005739 DNA topoisomerase I, archeal-type TopoI_arch Family
IPR005736 Reverse gyrase Reverse_gyrase Family
IPR005738 DNA topoisomerase III TopoIII Family

0 Parent Features

7 Publications

First Author Title Year Journal Volume Pages
Roca J The mechanisms of DNA topoisomerases. 1995 Trends Biochem Sci 20 156-60
Champoux JJ DNA topoisomerases: structure, function, and mechanism. 2001 Annu Rev Biochem 70 369-413
Gadelle D Phylogenomics of type II DNA topoisomerases. 2003 Bioessays 25 232-42
Wang JC Cellular roles of DNA topoisomerases: a molecular perspective. 2002 Nat Rev Mol Cell Biol 3 430-40
Aravind L Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins. 1998 Nucleic Acids Res 26 4205-13
Perry K Structure of a complex between E. coli DNA topoisomerase I and single-stranded DNA. 2003 Structure 11 1349-58
Mondragón A The structure of Escherichia coli DNA topoisomerase III. 1999 Structure 7 1373-83



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)