5t5c
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==A Novel domain in human EXOG converts apoptotic endonuclease to DNA-repair enzyme== | |
| + | <StructureSection load='5t5c' size='340' side='right' caption='[[5t5c]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5t5c]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T5C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T5C FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5t3v|5t3v]], [[5t40|5t40]], [[5t4i|5t4i]]</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=5t5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t5c OCA], [http://pdbe.org/5t5c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t5c RCSB], [http://www.ebi.ac.uk/pdbsum/5t5c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t5c ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/EXOG_HUMAN EXOG_HUMAN]] Endo/exonuclease with nicking activity towards supercoiled DNA, a preference for single-stranded DNA and 5'-3' exonuclease activity.<ref>PMID:18187503</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Human EXOG (hEXOG) is a 5'-exonuclease that is crucial for mitochondrial DNA repair; the enzyme belongs to a nonspecific nuclease family that includes the apoptotic endonuclease EndoG. Here we report biochemical and structural studies of hEXOG, including structures in its apo form and in a complex with DNA at 1.81 and 1.85 A resolution, respectively. A Wing domain, absent in other betabetaalpha-Me members, suppresses endonuclease activity, but confers on hEXOG a strong 5'-dsDNA exonuclease activity that precisely excises a dinucleotide using an intrinsic 'tape-measure'. The symmetrical apo hEXOG homodimer becomes asymmetrical upon binding to DNA, providing a structural basis for how substrate DNA bound to one active site allosterically regulates the activity of the other. These properties of hEXOG suggest a pathway for mitochondrial BER that provides an optimal substrate for subsequent gap-filling synthesis by DNA polymerase gamma. | ||
| - | + | A domain in human EXOG converts apoptotic endonuclease to DNA-repair exonuclease.,Szymanski MR, Yu W, Gmyrek AM, White MA, Molineux IJ, Lee JC, Yin YW Nat Commun. 2017 May 3;8:14959. doi: 10.1038/ncomms14959. PMID:28466855<ref>PMID:28466855</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Szymanski, M | + | <div class="pdbe-citations 5t5c" style="background-color:#fffaf0;"></div> |
| - | [[Category: Yin, W | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Szymanski, M R]] | ||
| + | [[Category: Yin, W Y]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Dna-repair]] | ||
| + | [[Category: Exonuclease]] | ||
| + | [[Category: Hydrolase-dna complex]] | ||
| + | [[Category: Mitochondria]] | ||
Revision as of 15:43, 17 May 2017
A Novel domain in human EXOG converts apoptotic endonuclease to DNA-repair enzyme
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