5gkc: Difference between revisions
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==The crystal structure of the CPS-6 H148A/F122A== | ==The crystal structure of the CPS-6 H148A/F122A== | ||
<StructureSection load='5gkc' size='340' side='right' caption='[[5gkc]], [[Resolution|resolution]] 1.89Å' scene=''> | <StructureSection load='5gkc' size='340' side='right'caption='[[5gkc]], [[Resolution|resolution]] 1.89Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5gkc]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5gkc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GKC FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.892Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5gkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gkc OCA], [https://pdbe.org/5gkc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gkc RCSB], [https://www.ebi.ac.uk/pdbsum/5gkc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gkc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/NUCG_CAEEL NUCG_CAEEL] Endonuclease important for programmed cell death; it mediates apoptotic DNA fragmentation. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 5gkc" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5gkc" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Endonuclease 3D structures|Endonuclease 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Caenorhabditis elegans]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Lin JL]] | ||
[[Category: | [[Category: Yuan HS]] | ||
Latest revision as of 14:34, 2 August 2023
The crystal structure of the CPS-6 H148A/F122AThe crystal structure of the CPS-6 H148A/F122A
Structural highlights
FunctionNUCG_CAEEL Endonuclease important for programmed cell death; it mediates apoptotic DNA fragmentation. Publication Abstract from PubMedEndonuclease G (EndoG) is an evolutionarily conserved mitochondrial protein in eukaryotes that digests nucleus chromosomal DNA during apoptosis and paternal mitochondrial DNA during embryogenesis. Under oxidative stress, homodimeric EndoG becomes oxidized and converts to monomers with diminished nuclease activity. However, it remains unclear why EndoG has to function as a homodimer in DNA degradation. Here, we report the crystal structure of the Caenorhabditis elegans EndoG homologue, CPS-6, in complex with single-stranded DNA at a resolution of 2.3 A. Two separate DNA strands are bound at the betabetaalpha-metal motifs in the homodimer with their nucleobases pointing away from the enzyme, explaining why CPS-6 degrades DNA without sequence specificity. Two obligatory monomeric CPS-6 mutants (P207E and K131D/F132N) were constructed, and they degrade DNA with diminished activity due to poorer DNA-binding affinity as compared to wild-type CPS-6. Moreover, the P207E mutant exhibits predominantly 3'-to-5' exonuclease activity, indicating a possible endonuclease to exonuclease activity change. Thus, the dimer conformation of CPS-6 is essential for maintaining its optimal DNA-binding and endonuclease activity. Compared to other non-specific endonucleases, which are usually monomeric enzymes, EndoG is a unique dimeric endonuclease, whose activity hence can be modulated by oxidation to induce conformational changes. Crystal structure of endonuclease G in complex with DNA reveals how it nonspecifically degrades DNA as a homodimer.,Lin JL, Wu CC, Yang WZ, Yuan HS Nucleic Acids Res. 2016 Dec 1;44(21):10480-10490. Epub 2016 Oct 13. PMID:27738134[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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