1zvt

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(New page: 200px<br /><applet load="1zvt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zvt, resolution 1.70&Aring;" /> '''Structure of the E. ...)
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[[Image:1zvt.gif|left|200px]]<br /><applet load="1zvt" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1zvt, resolution 1.70&Aring;" />
 
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'''Structure of the E. coli ParC C-terminal domain'''<br />
 
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==Overview==
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==Structure of the E. coli ParC C-terminal domain==
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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.
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<StructureSection load='1zvt' size='340' side='right'caption='[[1zvt]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1zvt]] is a 2 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=1ZVT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZVT FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zvt OCA], [https://pdbe.org/1zvt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zvt RCSB], [https://www.ebi.ac.uk/pdbsum/1zvt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zvt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zv/1zvt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1zvt ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1ZVT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZVT OCA].
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*[[Topoisomerase 3D structures|Topoisomerase 3D structures]]
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== References ==
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==Reference==
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<references/>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16023670 16023670]
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Berger, J.M.]]
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[[Category: Berger JM]]
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[[Category: Corbett, K.D.]]
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[[Category: Corbett KD]]
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[[Category: Schoeffler, A.J.]]
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[[Category: Schoeffler AJ]]
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[[Category: Thomsen, N.D.]]
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[[Category: Thomsen ND]]
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[[Category: atpase]]
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[[Category: beta-pinwheel]]
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[[Category: decatenation]]
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[[Category: dna binding]]
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[[Category: dna topology]]
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[[Category: supercoiling]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:41:29 2007''
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Current revision

Structure of the E. coli ParC C-terminal domain

PDB ID 1zvt

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