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[[Image:1zvu.gif|left|200px]]
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{{STRUCTURE_1zvu|  PDB=1zvu  |  SCENE=  }}
'''Structure of the full-length E. coli ParC subunit'''


==Structure of the full-length E. coli ParC subunit==
<StructureSection load='1zvu' size='340' side='right'caption='[[1zvu]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1zvu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZVU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zvu OCA], [https://pdbe.org/1zvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zvu RCSB], [https://www.ebi.ac.uk/pdbsum/1zvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zvu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PARC_ECOLI PARC_ECOLI] Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule. MukB stimulates the relaxation activity of topoisomerase IV and also has a modest effect on decatenation.<ref>PMID:20921377</ref> <ref>PMID:12269820</ref> <ref>PMID:21300644</ref> <ref>PMID:16023670</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zv/1zvu_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zvu ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Most bacteria possess two type IIA topoisomerases, DNA gyrase and topo IV, that together help manage chromosome integrity and topology. Gyrase primarily introduces negative supercoils into DNA, an activity mediated by the C-terminal domain of its DNA binding subunit (GyrA). Although closely related to gyrase, topo IV preferentially decatenates DNA and relaxes positive supercoils. Here we report the structure of the full-length Escherichia coli ParC dimer at 3.0 A resolution. The N-terminal DNA binding region of ParC is highly similar to that of GyrA, but the ParC dimer adopts a markedly different conformation. The C-terminal domain (CTD) of ParC is revealed to be a degenerate form of the homologous GyrA CTD, and is anchored to the top of the N-terminal domains in a configuration different from that thought to occur in gyrase. Biochemical assays show that the ParC CTD controls the substrate specificity of topo IV, likely by capturing DNA segments of certain crossover geometries. This work delineates strong mechanistic parallels between topo IV and gyrase, while explaining how structural differences between the two enzyme families have led to distinct activity profiles. These findings in turn explain how the structures and functions of bacterial type IIA topoisomerases have evolved to meet specific needs of different bacterial families for the control of chromosome superstructure.


==Overview==
The structural basis for substrate specificity in DNA topoisomerase IV.,Corbett KD, Schoeffler AJ, Thomsen ND, Berger JM J Mol Biol. 2005 Aug 19;351(3):545-61. PMID:16023670<ref>PMID:16023670</ref>
Most bacteria possess two type IIA topoisomerases, DNA gyrase and topo IV, that together help manage chromosome integrity and topology. Gyrase primarily introduces negative supercoils into DNA, an activity mediated by the C-terminal domain of its DNA binding subunit (GyrA). Although closely related to gyrase, topo IV preferentially decatenates DNA and relaxes positive supercoils. Here we report the structure of the full-length Escherichia coli ParC dimer at 3.0 A resolution. The N-terminal DNA binding region of ParC is highly similar to that of GyrA, but the ParC dimer adopts a markedly different conformation. The C-terminal domain (CTD) of ParC is revealed to be a degenerate form of the homologous GyrA CTD, and is anchored to the top of the N-terminal domains in a configuration different from that thought to occur in gyrase. Biochemical assays show that the ParC CTD controls the substrate specificity of topo IV, likely by capturing DNA segments of certain crossover geometries. This work delineates strong mechanistic parallels between topo IV and gyrase, while explaining how structural differences between the two enzyme families have led to distinct activity profiles. These findings in turn explain how the structures and functions of bacterial type IIA topoisomerases have evolved to meet specific needs of different bacterial families for the control of chromosome superstructure.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1ZVU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZVU OCA].
</div>
<div class="pdbe-citations 1zvu" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
The structural basis for substrate specificity in DNA topoisomerase IV., Corbett KD, Schoeffler AJ, Thomsen ND, Berger JM, J Mol Biol. 2005 Aug 19;351(3):545-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16023670 16023670]
*[[Topoisomerase 3D structures|Topoisomerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Berger, J M.]]
[[Category: Berger JM]]
[[Category: Corbett, K D.]]
[[Category: Corbett KD]]
[[Category: Schoeffler, A J.]]
[[Category: Schoeffler AJ]]
[[Category: Thomsen, N D.]]
[[Category: Thomsen ND]]
[[Category: Atpase]]
[[Category: Beta-pinwheel]]
[[Category: Decatenation]]
[[Category: Dna binding]]
[[Category: Dna topology]]
[[Category: Supercoiling]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:08:23 2008''

Latest revision as of 07:15, 23 August 2023

Structure of the full-length E. coli ParC subunit

1zvu, resolution 3.00Å

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