View source for 5t40


==A Novel domain in human EXOG converts apoptotic endonuclease to DNA-repair enzyme==
<StructureSection load='5t40' size='340' side='right'caption='[[5t40]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5t40]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T40 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.81&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5t40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t40 OCA], [https://pdbe.org/5t40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t40 RCSB], [https://www.ebi.ac.uk/pdbsum/5t40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t40 ProSAT]</span></td></tr>
</table>
== Function ==
[https://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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5t40" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Szymanski MR]]
[[Category: Yin WY]]