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| | <StructureSection load='4wa8' size='340' side='right'caption='[[4wa8]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='4wa8' size='340' side='right'caption='[[4wa8]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wa8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Metka Metka]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WA8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WA8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wa8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanopyrus_kandleri_AV19 Methanopyrus kandleri AV19]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WA8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fen, MK0566 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=190192 METKA])</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=4wa8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wa8 OCA], [https://pdbe.org/4wa8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wa8 RCSB], [https://www.ebi.ac.uk/pdbsum/4wa8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wa8 ProSAT]</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=4wa8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wa8 OCA], [http://pdbe.org/4wa8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wa8 RCSB], [http://www.ebi.ac.uk/pdbsum/4wa8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wa8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FEN_METKA FEN_METKA]] Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA (By similarity). | + | [https://www.uniprot.org/uniprot/FEN_METKA FEN_METKA] Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Endonuclease|Endonuclease]] | + | *[[Endonuclease 3D structures|Endonuclease 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Metka]] | + | [[Category: Methanopyrus kandleri AV19]] |
| - | [[Category: Dunten, P]] | + | [[Category: Dunten P]] |
| - | [[Category: Horton, N C]] | + | [[Category: Horton NC]] |
| - | [[Category: Shah, S]] | + | [[Category: Shah S]] |
| - | [[Category: Dna nuclease]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Nucleotide excision repair]]
| + | |
| Structural highlights
Function
FEN_METKA Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA (By similarity).
Publication Abstract from PubMed
DNA repair is fundamental to genome stability and is found in all three domains of life. However, many archaeal species, such as Methanopyrus kandleri, contain only a subset of the eukaryotic nucleotide excision repair (NER) homologues, and those present often contain significant differences compared to their eukaryotic homologues. To clarify the role of the NER XPG-like protein Mk0566 from M. kandleri, its biochemical activity and three dimensional structure were investigated. Both were found to be more similar to human FEN-1 than human XPG, suggesting a biological role in replication and long-patch base excision repair rather than in NER. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc.
Structure and Specificity of FEN-1 from Methanopyrus kandleri.,Shah S, Dunten P, Stiteler A, Park CK, Horton NC Proteins. 2014 Oct 30. doi: 10.1002/prot.24704. PMID:25354467[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shah S, Dunten P, Stiteler A, Park CK, Horton NC. Structure and Specificity of FEN-1 from Methanopyrus kandleri. Proteins. 2014 Oct 30. doi: 10.1002/prot.24704. PMID:25354467 doi:http://dx.doi.org/10.1002/prot.24704
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