5c5j

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'''Unreleased structure'''
 
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The entry 5c5j is ON HOLD until Paper Publication
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==Poymerase Nucleotide complex==
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<StructureSection load='5c5j' size='340' side='right' caption='[[5c5j]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5c5j]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C5J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C5J FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8GT:8-OXO-GUANOSINE-5-TRIPHOSPHATE'>8GT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5c5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c5j OCA], [http://pdbe.org/5c5j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c5j RCSB], [http://www.ebi.ac.uk/pdbsum/5c5j PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/W8STT9_ECOLX W8STT9_ECOLX]] Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.[SAAS:SAAS00538441] Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.[HAMAP-Rule:MF_01113]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Recent studies posit that reactive oxygen species (ROS) contribute to the cell lethality of bactericidal antibiotics. However, this conjecture has been challenged and remains controversial. To resolve this controversy, we adopted a strategy that involves DNA polymerase IV (PolIV). The nucleotide pool of the cell gets oxidized by ROS and PolIV incorporates the damaged nucleotides (especially 8oxodGTP) into the genome, which results in death of the bacteria. By using a combination of structural and biochemical tools coupled with growth assays, it was shown that selective perturbation of the 8oxodGTP incorporation activity of PolIV results in considerable enhancement of the survival of bacteria in the presence of the norfloxacin antibiotic. Our studies therefore indicate that ROS induced in bacteria by the presence of antibiotics in the environment contribute significantly to cell lethality.
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Authors: Nair, D.T., Kottur, J.
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Reactive Oxygen Species Play an Important Role in the Bactericidal Activity of Quinolone Antibiotics.,Kottur J, Nair DT Angew Chem Int Ed Engl. 2016 Feb 12;55(7):2397-400. doi: 10.1002/anie.201509340. , Epub 2016 Jan 12. PMID:26757158<ref>PMID:26757158</ref>
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Description: Poymerase Nucleotide complex
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Nair, D.T]]
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<div class="pdbe-citations 5c5j" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: DNA-directed DNA polymerase]]
[[Category: Kottur, J]]
[[Category: Kottur, J]]
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[[Category: Nair, D T]]
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[[Category: Dna polymerase]]
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[[Category: Replication]]
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[[Category: Transferase-dna complex]]

Revision as of 23:12, 23 June 2016

Poymerase Nucleotide complex

5c5j, resolution 2.10Å

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