4e09

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Current revision (11:01, 1 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4e09]] 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=4E09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E09 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4e09]] 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=4E09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E09 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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]] 2.99&#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=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4e09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e09 OCA], [https://pdbe.org/4e09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e09 RCSB], [https://www.ebi.ac.uk/pdbsum/4e09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e09 ProSAT]</span></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=4e09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e09 OCA], [https://pdbe.org/4e09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e09 RCSB], [https://www.ebi.ac.uk/pdbsum/4e09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e09 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/B0ZE06_ECOLX B0ZE06_ECOLX]]
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[https://www.uniprot.org/uniprot/B0ZE06_ECOLX B0ZE06_ECOLX]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Segregation of the bacterial multidrug resistance plasmid TP228 requires the centromere-binding protein, ParG the parH centromere and the Walker-box ATPase, ParF. The cycling of ParF between ADP and ATP bound states drives TP228 partition; ATP binding stimulates ParF polymerization, which is essential for segregation while ADP binding antagonizes polymerization and inhibits DNA partition. The molecular mechanism involved in this adenine nucleotide switch is unclear. Moreover, it is unknown how any Walker-box protein polymerizes in an ATP-dependent manner. Here we describe multiple ParF structures in ADP and AMPPCP bound states. ParF-ADP is monomeric but dimerizes when complexed with AMPPCP. Strikingly, in ParF-AMPPCP structures, the dimers interact to create dimer-of-dimers units that generate a specific linear filament. Mutation of interface residues prevents both polymerization and DNA segregation in vivo. Thus, these data reveal the unique mechanism by which a Walker-box protein forms polymers that involves the generation of ATP-induced dimer-of-dimer building blocks.
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Structural mechanism of ATP induced polymerization of the partition factor ParF: implications for DNA segregation.,Schumacher MA, Ye Q, Barge MT, Zampini M, Barilla D, Hayes F J Biol Chem. 2012 Jun 6. PMID:22674577<ref>PMID:22674577</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4e09" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Structure of ParF-AMPPCP, I422 form

PDB ID 4e09

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