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| ==Structure of Prim-PolC from Mycobacterium smegmatis== | | ==Structure of Prim-PolC from Mycobacterium smegmatis== |
- | <StructureSection load='5op0' size='340' side='right' caption='[[5op0]], [[Resolution|resolution]] 1.84Å' scene=''> | + | <StructureSection load='5op0' size='340' side='right'caption='[[5op0]], [[Resolution|resolution]] 1.84Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5op0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs2 Mycs2]. 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> | + | <table><tr><td colspan='2'>[[5op0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5OP0 FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ligD, MSMEG_6301 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84Å</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> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5op0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5op0 OCA], [https://pdbe.org/5op0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5op0 RCSB], [https://www.ebi.ac.uk/pdbsum/5op0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5op0 ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/A0R5T1_MYCS2 A0R5T1_MYCS2] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Mycs2]] | + | [[Category: Large Structures]] |
- | [[Category: Brissett, N C]] | + | [[Category: Mycolicibacterium smegmatis MC2 155]] |
- | [[Category: Doherty, A J]] | + | [[Category: Brissett NC]] |
- | [[Category: Base excision repair]] | + | [[Category: Doherty AJ]] |
- | [[Category: Nucleotidyl transferase]]
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- | [[Category: Polymerase]]
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- | [[Category: Transferase]]
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| Structural highlights
Function
A0R5T1_MYCS2
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Plocinski P, Brissett NC, Bianchi J, Brzostek A, Korycka-Machala M, Dziembowski A, Dziadek J, Doherty AJ. DNA Ligase C and Prim-PolC participate in base excision repair in mycobacteria. Nat Commun. 2017 Nov 1;8(1):1251. doi: 10.1038/s41467-017-01365-y. PMID:29089537 doi:http://dx.doi.org/10.1038/s41467-017-01365-y
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