Topoisomerase

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__TOC__
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==Function==
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[[Topoisomerase]] (TOP) winds and unwinds DNA double helix in order to enable DNA replication.<br />
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[[Topoisomerase]] (TOP) winds and unwinds DNA double helix in order to enable DNA replication. The reaction catalyzed by topoisomerases leads to the conversion of one topological isomer of DNA to another.<br />
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* '''TOPI''' cuts one strand of the double helix. It has 3 subclasses: TOPIA which shares its mechanism with TOPII and TOPIB which uses rotary mechanism and includes topo I and topo III. TOPIC called TOPV shares its mechanism with TOPIB but is structurally unique.<br />
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* '''TOPI''' cuts one strand of the double helix. It has 3 subclasses: TOPIA which shares its mechanism with TOPII and TOPIB which uses rotary mechanism and includes topo I and topo III. TOPIC called TOPV shares its mechanism with TOPIB but is structurally unique. See also [[Variola Topoisomerase 1B]] and [[Smallpox (Variola Virus) - Topoisomerase 1B]].<br />
* '''TOPII''' cuts both strands of the double helix. Its subclasses are TOPIIA including topo II and TOPIIB which includes topo VI.<br />
* '''TOPII''' cuts both strands of the double helix. Its subclasses are TOPIIA including topo II and TOPIIB which includes topo VI.<br />
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* '''TOPIII''' is a potent decatenase.<br />
* '''TOPIV''' is a type of TOPII, contains an ATP-binding domain ParE and a catalytic domain ParC.<br />
* '''TOPIV''' is a type of TOPII, contains an ATP-binding domain ParE and a catalytic domain ParC.<br />
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See also [[Variola Topoisomerase 1B]] and [[Smallpox (Variola Virus) Topoisomerase 1B]].
 
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__TOC__
 
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==Function==
 
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The reaction catalyzed by topoisomerases leads to the conversion of one topological isomer of DNA to another. TOP3 is a potent decatenase.
 
==GO Annotations==
==GO Annotations==

Revision as of 13:07, 10 January 2016

Image:2f4q.png
Crystal Structure of Topoisomerase 2f4q

Template:STRUCTURE 2h7f











Contents

Function

Topoisomerase (TOP) winds and unwinds DNA double helix in order to enable DNA replication. The reaction catalyzed by topoisomerases leads to the conversion of one topological isomer of DNA to another.

  • TOPI cuts one strand of the double helix. It has 3 subclasses: TOPIA which shares its mechanism with TOPII and TOPIB which uses rotary mechanism and includes topo I and topo III. TOPIC called TOPV shares its mechanism with TOPIB but is structurally unique. See also Variola Topoisomerase 1B and Smallpox (Variola Virus) - Topoisomerase 1B.
  • TOPII cuts both strands of the double helix. Its subclasses are TOPIIA including topo II and TOPIIB which includes topo VI.
  • TOPIII is a potent decatenase.
  • TOPIV is a type of TOPII, contains an ATP-binding domain ParE and a catalytic domain ParC.

GO Annotations

Database ID Symbol Qualifier GO Identifier GO Term Name Aspect Evidence Reference With Taxon Date Assigned by Product Form ID
UniProtKB P14294 topB GO:0006259 DNA metabolic process P IEA InterPro2GO InterPro:IPR006154 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006265 DNA topological change P IEA InterPro2GO InterPro:IPR000380 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006265 DNA topological change P IEA InterPro2GO InterPro:IPR003601 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006265 DNA topological change P IEA InterPro2GO InterPro:IPR003602 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006265 DNA topological change P IEA InterPro2GO InterPro:IPR005738 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006265 DNA topological change P IEA InterPro2GO InterPro:IPR013497 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006265 DNA topological change P IEA InterPro2GO InterPro:IPR013824 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006265 DNA topological change P IEA InterPro2GO InterPro:IPR013825 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006268 DNA unwinding involved in replication P IEA InterPro2GO InterPro:IPR013824 83333 20101127 InterPro
UniProtKB P14294 topB GO:0006268 DNA unwinding involved in replication P IEA InterPro2GO InterPro:IPR013825 83333 20101127 InterPro
UniProtKB P14294 topB GO:0000166 nucleotide binding F IEA Swiss-Prot Keywords2GO SP_KW:KW-0547 83333 20101127 UniProtKB
UniProtKB P14294 topB GO:0003676 nucleic acid binding F IEA InterPro2GO InterPro:IPR006154 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003677 DNA binding F IEA InterPro2GO InterPro:IPR000380 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003677 DNA binding F IEA InterPro2GO InterPro:IPR003601 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003677 DNA binding F IEA InterPro2GO InterPro:IPR003602 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003677 DNA binding F IEA InterPro2GO InterPro:IPR005738 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003677 DNA binding F IEA InterPro2GO InterPro:IPR013497 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003677 DNA binding F IEA InterPro2GO InterPro:IPR013824 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003677 DNA binding F IEA InterPro2GO InterPro:IPR013825 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003677 DNA binding F IEA Swiss-Prot Keywords2GO SP_KW:KW-0238 83333 20101127 UniProtKB
UniProtKB P14294 topB GO:0003916 DNA topoisomerase activity F IEA InterPro2GO InterPro:IPR003601 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003916 DNA topoisomerase activity F IEA InterPro2GO InterPro:IPR003602 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003916 DNA topoisomerase activity F IEA InterPro2GO InterPro:IPR005738 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003916 DNA topoisomerase activity F IEA InterPro2GO InterPro:IPR013497 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003916 DNA topoisomerase activity F IEA InterPro2GO InterPro:IPR013824 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003916 DNA topoisomerase activity F IEA InterPro2GO InterPro:IPR013825 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003916 DNA topoisomerase activity F IEA Swiss-Prot Keywords2GO SP_KW:KW-0799 83333 20101127 UniProtKB
UniProtKB P14294 topB GO:0003917 DNA topoisomerase type I activity F IDA PMID:6326814 83333 20100621 EcoliWiki
UniProtKB P14294 topB GO:0003917 DNA topoisomerase type I activity F IEA InterPro2GO InterPro:IPR000380 83333 20101127 InterPro
UniProtKB P14294 topB GO:0003917 DNA topoisomerase type I activity F IEA EC2GO EC:5.99.1.2 83333 20100703 UniProtKB
UniProtKB P14294 topB GO:0005515 protein binding F IPI PMID:15690043 frlR (FRLR_ECOLI) 83333 20101127 IntAct
UniProtKB P14294 topB GO:0005524 ATP binding F IEA Swiss-Prot Keywords2GO SP_KW:KW-0067 83333 20101127 UniProtKB
UniProtKB P14294 topB GO:0016853 isomerase activity F IEA Swiss-Prot Keywords2GO SP_KW:KW-0413 83333 20101127 UniProtKB
UniProtKB P14294 topB GO:0005694 chromosome C IEA InterPro2GO InterPro:IPR000380 83333 20101127 InterPro
UniProtKB P14294 topB GO:0005694 chromosome C IEA InterPro2GO InterPro:IPR003601 83333 20101127 InterPro
UniProtKB P14294 topB GO:0005694 chromosome C IEA InterPro2GO InterPro:IPR003602 83333 20101127 InterPro
UniProtKB P14294 topB GO:0005694 chromosome C IEA InterPro2GO InterPro:IPR005738 83333 20101127 InterPro
UniProtKB P14294 topB GO:0005694 chromosome C IEA InterPro2GO InterPro:IPR013497 83333 20101127 InterPro
UniProtKB P14294 topB GO:0005694 chromosome C IEA InterPro2GO InterPro:IPR013824 83333 20101127 InterPro
UniProtKB P14294 topB GO:0005694 chromosome C IEA InterPro2GO InterPro:IPR013825 83333 20101127 InterPro

Copied from [1] Last updated Dec 2 2010


3D Structures of Topoisomerase

Updated on 10-January-2016


Created with the participation of Sonny Zhao.

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Joel L. Sussman, Alexander Berchansky, Jaime Prilusky

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