5op0

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m (Protected "5op0" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5op0 is ON HOLD until Paper Publication
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==Structure of Prim-PolC from Mycobacterium smegmatis==
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<StructureSection load='5op0' size='340' side='right' caption='[[5op0]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5op0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OP0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OP0 FirstGlance]. <br>
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</td></tr><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=5op0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5op0 OCA], [http://pdbe.org/5op0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5op0 RCSB], [http://www.ebi.ac.uk/pdbsum/5op0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5op0 ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Prokaryotic Ligase D is a conserved DNA repair apparatus processing DNA double-strand breaks in stationary phase. An orthologous Ligase C (LigC) complex also co-exists in many bacterial species but its function is unknown. Here we show that the LigC complex interacts with core BER enzymes in vivo and demonstrate that together these factors constitute an excision repair apparatus capable of repairing damaged bases and abasic sites. The polymerase component, which contains a conserved C-terminal structural loop, preferentially binds to and fills-in short gapped DNA intermediates with RNA and LigC ligates the resulting nicks to complete repair. Components of the LigC complex, like LigD, are expressed upon entry into stationary phase and cells lacking either of these pathways exhibit increased sensitivity to oxidising genotoxins. Together, these findings establish that the LigC complex is directly involved in an excision repair pathway(s) that repairs DNA damage with ribonucleotides during stationary phase.
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Authors: Brissett, N.C., Doherty, A.J.
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DNA Ligase C and Prim-PolC participate in base excision repair in mycobacteria.,Plocinski P, Brissett NC, Bianchi J, Brzostek A, Korycka-Machala M, Dziembowski A, Dziadek J, Doherty AJ Nat Commun. 2017 Nov 1;8(1):1251. doi: 10.1038/s41467-017-01365-y. PMID:29089537<ref>PMID:29089537</ref>
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Description: Structure of Prim-PolC from Mycobacterium smegmatis
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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: Brissett, N.C]]
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<div class="pdbe-citations 5op0" style="background-color:#fffaf0;"></div>
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[[Category: Doherty, A.J]]
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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: Brissett, N C]]
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[[Category: Doherty, A J]]
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[[Category: Base excision repair]]
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[[Category: Nucleotidyl transferase]]
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[[Category: Polymerase]]
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[[Category: Transferase]]

Revision as of 07:30, 15 November 2017

Structure of Prim-PolC from Mycobacterium smegmatis

5op0, resolution 1.84Å

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