User:Isabelle Kressy/Sandbox 1

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== Evolutionarily Related Proteins ==
== Evolutionarily Related Proteins ==
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<Structure load='4Z2D' size='350' frame='true' align='left' caption='''S. pneumoniae''Gyrase DNA cleavage complex with Quinolone' />
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<Structure load='4Z2D' size='350' frame='true' align='left' caption='Gyrase DNA cleavage complex with Quinolone' />
== Available Structures ==
== Available Structures ==

Revision as of 21:51, 2 May 2022

Contents

Quinolone(Clinafloxacin)-DNA cleavage complex of type IV topoisomerase from S. pneumoniae

Type IV topoisomerase DNA cleavage complex with Quinolone. PDB ID: 3RAD

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Topoisomerase IV in S. pneumoniae is a paralogue of type II topoisomerase. This structure is a complex of topoisomerase, DNA, and Quinolone, a drug that targets type II topoisomerases in Gram-negative and Gram-positive bacteria [1]. Topoisomerase IV consists of two subunits that function to regulate supercoiling and disentangle DNA.

Function

The main function of topoisomerase IV is to regulate the level of DNA supercoiling within the cell so that replication, transcription, and repair can take place [2].

In general, type II topoisomerases undergo a strand-passage mechanism to remove supercoiling and disentangle chromosomes. These enzymes cleave both strands of DNA and then pass a second duplex through the break using ATP. The cleaved strands are ligated together again and the two products are released from the enzyme [3].

Structural Description

The active site is a tetramer made up of and subunits. The ParC subunit contains an N-terminal DNA breakage-reunion domain, which is linked to C-terminal β-pinwheel domains. This favors the passage of DNA and DNA unlinking from the complex. In contrast, the N-terminal of the ParE subunits forms the ATPase domain. Topoisomerase IV forms a complex with gyrase and works in tandem to remove DNA supercoiling and disentangle chromosomes.

Structure Insights

Evolutionarily Related Proteins

Gyrase DNA cleavage complex with Quinolone

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Available Structures

</StructureSection>

References

  1. Laponogov I, Pan XS, Veselkov DA, Cirz RT, Wagman A, Moser HE, Fisher LM, Sanderson MR. Exploring the active site of the Streptococcus pneumoniae topoisomerase IV-DNA cleavage complex with novel 7,8-bridged fluoroquinolones. Open Biol. 2016 Sep;6(9). pii: rsob.160157. doi: 10.1098/rsob.160157. PMID:27655731 doi:http://dx.doi.org/10.1098/rsob.160157
  2. Laponogov I, Pan XS, Veselkov DA, Cirz RT, Wagman A, Moser HE, Fisher LM, Sanderson MR. Exploring the active site of the Streptococcus pneumoniae topoisomerase IV-DNA cleavage complex with novel 7,8-bridged fluoroquinolones. Open Biol. 2016 Sep;6(9). pii: rsob.160157. doi: 10.1098/rsob.160157. PMID:27655731 doi:http://dx.doi.org/10.1098/rsob.160157
  3. Laponogov I, Veselkov DA, Crevel IM, Pan XS, Fisher LM, Sanderson MR. Structure of an 'open' clamp type II topoisomerase-DNA complex provides a mechanism for DNA capture and transport. Nucleic Acids Res. 2013 Aug 21. PMID:23965305 doi:10.1093/nar/gkt749

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Isabelle Kressy

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