InterPro : IPR006691

Name  DNA gyrase/topoisomerase IV, subunit A, C-terminal beta-pinwheel Short Name  GyrA/parC_pinwhl
Type  Repeat 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 II topoisomerases are ATP-dependent enzymes, and can be subdivided according to their structure and reaction mechanisms: type IIA (topoisomerase II or gyrase, and topoisomerase IV) and type IIB (topoisomerase VI). These enzymes are responsible for relaxing supercoiled DNA as well as for introducing both negative and positive supercoils [].This entry represents the beta-pinwheel repeat found at the C-terminal end of subunit A of topoisomerase IV (ParC) and subunit A of DNA gyrase (GyrA). DNA gyrase is the topoisomerase II found primarily in bacteria and archaea that consists of two polypeptide subunits, gyrA and gyrB, which form a heterotetramer: (BA)2. This is distinct from the topoisomerase II found in most eukaryotes, which consists of a single polypeptide, with the N- and C-terminal regions corresponding to gyrB and gyrA, respectively, and which is not represented in this entry.The ability of DNA gyrase to introduce negative supercoils into DNA is mediated in part by the C-terminal domain of subunit A, which forms a beta-pinwheel fold that is similar to a beta-propeller but with a different blade topology, and which forms a superhelical spiral domain [, ]. This beta-pinwheel is capable of bending DNA by over 180 degrees over a 40 bp region, possibly by wrapping the DNA around the GyrA C-terminal beta-pinwheel domain.In topoisomerase IV, although the C-terminal domain forms a similar superhelical spiral to that of DNA gyrase A, it assembles as a broken form of a beta-pinwheel as distinct from that of gyrA, due to the absence of a DNA gyrase-specific GyrA box motif []. This difference may account for parC being less efficient than gyrA in mediating DNA-bending, leading to their divergence in terms of activity, where topoisomerase IV acts to relax positive supercoils, and DNA gyrase acts to introduce negative supercoils [].
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Proteins

InterPro protein domain ID --> Contigs

 

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1 Found In

Id Name Short Name Type
IPR002205 DNA topoisomerase, type IIA, subunit A/C-terminal Topo_IIA_A/C Domain

0 Parent Features

9 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
Watt PM Structure and function of type II DNA topoisomerases. 1994 Biochem J 303 ( Pt 3) 681-95
Corbett KD The structural basis for substrate specificity in DNA topoisomerase IV. 2005 J Mol Biol 351 545-61
Corbett KD The C-terminal domain of DNA gyrase A adopts a DNA-bending beta-pinwheel fold. 2004 Proc Natl Acad Sci U S A 101 7293-8
Ruthenburg AJ A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling bias. 2005 J Biol Chem 280 26177-84
Hsieh TJ Structure of the topoisomerase IV C-terminal domain: a broken beta-propeller implies a role as geometry facilitator in catalysis. 2004 J Biol Chem 279 55587-93



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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)