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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''==
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<StructureSection load='3rad' size='340' frame='true' align='right' caption='Type IV topoisomerase DNA cleavage complex with Quinolone. PDBID: 3RAD'/>
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<StructureSection load='3rad' size='340' frame='true' align='right' caption='Type IV topoisomerase DNA cleavage complex with Quinolone. PDB ID: 3RAD'/>
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

Revision as of 14:09, 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

Drag the structure with the mouse to rotate

You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.

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 [3].

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 [4].

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

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>

References

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
  3. 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
  4. 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

Proteopedia Page Contributors and Editors (what is this?)

Isabelle Kressy

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