1s14

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(New page: 200px<br /><applet load="1s14" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s14, resolution 2.0&Aring;" /> '''Crystal structure of ...)
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[[Image:1s14.gif|left|200px]]<br /><applet load="1s14" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1s14, resolution 2.0&Aring;" />
 
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'''Crystal structure of Escherichia coli Topoisomerase IV ParE 24kDa subunit'''<br />
 
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==Overview==
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==Crystal structure of Escherichia coli Topoisomerase IV ParE 24kDa subunit==
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Topoisomerase IV and DNA gyrase are related bacterial type II, topoisomerases that utilize the free energy from ATP hydrolysis to, catalyze topological changes in the bacterial genome. The essential, function of DNA gyrase is the introduction of negative DNA supercoils into, the genome, whereas the essential function of topoisomerase IV is to, decatenate daughter chromosomes following replication. Here, we report the, crystal structures of a 43-kDa N-terminal fragment of Escherichia coli, topoisomerase IV ParE subunit complexed with adenylyl-imidodiphosphate at, 2.0-A resolution and a 24-kDa N-terminal fragment of the ParE subunit, complexed with novobiocin at 2.1-A resolution. The solved ParE structures, are strikingly similar to the known gyrase B (GyrB) subunit structures. We, also identified single-position equivalent amino acid residues in ParE, (M74) and in GyrB (I78) that, when exchanged, increased the potency of, novobiocin against topoisomerase IV by nearly 20-fold (to 12 nM). The, corresponding exchange in gyrase (I78 M) yielded a 20-fold decrease in the, potency of novobiocin (to 1.0 micro M). These data offer an explanation, for the observation that novobiocin is significantly less potent against, topoisomerase IV than against DNA gyrase. Additionally, the enzyme kinetic, parameters were affected. In gyrase, the ATP K(m) increased approximately, 5-fold and the V(max) decreased approximately 30%. In contrast, the, topoisomerase IV ATP K(m) decreased by a factor of 6, and the V(max), increased approximately 2-fold from the wild-type values. These data, demonstrate that the ParE M74 and GyrB I78 side chains impart opposite, effects on the enzyme's substrate affinity and catalytic efficiency.
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<StructureSection load='1s14' size='340' side='right'caption='[[1s14]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1s14]] 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=1S14 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S14 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]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NOV:NOVOBIOCIN'>NOV</scene></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=1s14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s14 OCA], [https://pdbe.org/1s14 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s14 RCSB], [https://www.ebi.ac.uk/pdbsum/1s14 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s14 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PARE_ECOLI PARE_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:21300644</ref> <ref>PMID:15105144</ref> <ref>PMID:20921377</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/s1/1s14_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=1s14 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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1S14 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with NOV as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S14 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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Crystal structures of Escherichia coli topoisomerase IV ParE subunit (24 and 43 kilodaltons): a single residue dictates differences in novobiocin potency against topoisomerase IV and DNA gyrase., Bellon S, Parsons JD, Wei Y, Hayakawa K, Swenson LL, Charifson PS, Lippke JA, Aldape R, Gross CH, Antimicrob Agents Chemother. 2004 May;48(5):1856-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15105144 15105144]
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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: Gross, C.H.]]
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[[Category: Gross CH]]
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[[Category: Wei, Y.]]
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[[Category: Wei Y]]
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[[Category: NOV]]
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[[Category: alpha/beta globular protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:01:34 2007''
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Current revision

Crystal structure of Escherichia coli Topoisomerase IV ParE 24kDa subunit

PDB ID 1s14

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