TOP1BcBacterial DNA topoisomeraes I ATP-binding domain
|SMART accession number:||SM00436|
|Description:||Extension of TOPRIM in Bacterial DNA topoisomeraes I and III, Eukaryotic DNA topoisomeraes III, reverse gyrase beta subunit|
|Interpro abstract (IPR003601):|
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 [(PUBMED:7770916)]. 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 [(PUBMED:12042765), (PUBMED:11395412)]. DNA topoisomerases are divided into two classes: type I enzymes (EC 188.8.131.52; topoisomerases I, III and V) break single-strand DNA, and type II enzymes (EC 184.108.40.206; topoisomerases II, IV and VI) break double-strand DNA [(PUBMED:12596227)].
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 [(PUBMED:14604525), (PUBMED:10574789)]. The Toprim domain (IPR006171) forms a compact Rossmann fold that coordinates the Mg+2 ion [(PUBMED:9722641)].
|GO process:||DNA topological change (GO:0006265)|
|GO function:||DNA topoisomerase activity (GO:0003916), DNA binding (GO:0003677)|
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