6p0c: Difference between revisions

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-'''Unreleased structure'''
-The entry 6p0c is ON HOLD  until Paper Publication
+==Human DNA Ligase 1 Bound to an Adenylated, hydroxyl terminated DNA nick in EDTA==
+<StructureSection load='6p0c' size='340' side='right'caption='[[6p0c]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6p0c]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P0C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6P0C FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_ligase_(ATP) DNA ligase (ATP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.5.1.1 6.5.1.1] </span></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=6p0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p0c OCA], [http://pdbe.org/6p0c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p0c RCSB], [http://www.ebi.ac.uk/pdbsum/6p0c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p0c ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/DNLI1_HUMAN DNLI1_HUMAN]] DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+DNA ligases catalyze the joining of DNA strands to complete DNA replication, recombination and repair transactions. To protect the integrity of the genome, DNA ligase 1 (LIG1) discriminates against DNA junctions harboring mutagenic 3'-DNA mismatches or oxidative DNA damage, but how such high-fidelity ligation is enforced is unknown. Here, X-ray structures and kinetic analyses of LIG1 complexes with undamaged and oxidatively damaged DNA unveil that LIG1 employs Mg(2+)-reinforced DNA binding to validate DNA base pairing during the adenylyl transfer and nick-sealing ligation reaction steps. Our results support a model whereby LIG1 fidelity is governed by a high-fidelity (HiFi) interface between LIG1, Mg(2+), and the DNA substrate that tunes the enzyme to release pro-mutagenic DNA nicks. In a second tier of protection, LIG1 activity is surveilled by Aprataxin (APTX), which suppresses mutagenic and abortive ligation at sites of oxidative DNA damage.
-Authors:
+Two-tiered enforcement of high-fidelity DNA ligation.,Tumbale PP, Jurkiw TJ, Schellenberg MJ, Riccio AA, O'Brien PJ, Williams RS Nat Commun. 2019 Nov 28;10(1):5431. doi: 10.1038/s41467-019-13478-7. PMID:31780661<ref>PMID:31780661</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6p0c" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Riccio, A A]]
+[[Category: Schellenberg, M J]]
+[[Category: Tumbale, P S]]
+[[Category: Williams, R S]]
+[[Category: Adenylation domain]]
+[[Category: Dna binding domain]]
+[[Category: Ligase]]
+[[Category: Ligase-dna complex]]
+[[Category: Metalloenzyme]]
+[[Category: Ob fold]]
+[[Category: Phosphotransferase]]
+[[Category: Protein-dna complex]]