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==Quinolone(Clinafloxacin)-DNA cleavage complex of type IV topoisomerase from ''S. pneumoniae''==
==Quinolone(Clinafloxacin)-DNA cleavage complex of type IV topoisomerase from ''S. pneumoniae''==
<StructureSection load='3rad' size='340' frame='true' align='right' caption='Type IV topoisomerase DNA cleavage complex with Quinolone. PDB ID: 3RAD'/>
<StructureSection load='3rad' size='340' frame='true' align='right' caption='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. Topoisomerase IV consists of two subunits that function to regulate supercoiling and disentangle DNA.
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== Function ==
== Function ==

Revision as of 17:39, 27 April 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. Topoisomerase IV consists of two subunits that function to regulate supercoiling and disentangle DNA.


Function

Topoisomerase IV in S. pneumoniae is a paralogue of type II topoisomerase. Its main function is to regulate the level of DNA supercoiling within the cell so that replication, transcription, and repair can take place [1].

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 [2].

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

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, 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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