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{{STRUCTURE_4ny8|  PDB=4ny8  |  SCENE=  }}
===DNA polymerase beta with O6mG in the template base opposite to incoming non-hydrolyzable CTP with manganese in the active site===
{{ABSTRACT_PUBMED_24694247}}


==Function==
==DNA polymerase beta with O6mG in the template base opposite to incoming non-hydrolyzable CTP with manganese in the active site==
[[http://www.uniprot.org/uniprot/DPOLB_HUMAN DPOLB_HUMAN]] Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.<ref>PMID:9207062</ref> <ref>PMID:9572863</ref> <ref>PMID:11805079</ref> <ref>PMID:21362556</ref>
<StructureSection load='4ny8' size='340' side='right'caption='[[4ny8]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ny8]] is a 4 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=4NY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NY8 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]] 2.246&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0KX:2-DEOXY-5-O-[(R)-HYDROXY{[(R)-HYDROXY(PHOSPHONOOXY)PHOSPHORYL]AMINO}PHOSPHORYL]CYTIDINE'>0KX</scene>, <scene name='pdbligand=6OG:6-O-METHYL+GUANOSINE-5-MONOPHOSPHATE'>6OG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4ny8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ny8 OCA], [https://pdbe.org/4ny8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ny8 RCSB], [https://www.ebi.ac.uk/pdbsum/4ny8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ny8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DPOLB_HUMAN DPOLB_HUMAN] Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.<ref>PMID:9207062</ref> <ref>PMID:9572863</ref> <ref>PMID:11805079</ref> <ref>PMID:21362556</ref>  


==About this Structure==
==See Also==
[[4ny8]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NY8 OCA].
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:024694247</ref><references group="xtra"/><references/>
__TOC__
[[Category: Koag, M C.]]
</StructureSection>
[[Category: Lee, S.]]
[[Category: Homo sapiens]]
[[Category: Min, K.]]
[[Category: Large Structures]]
[[Category: Monzingo, A F.]]
[[Category: Koag M-C]]
[[Category: Dna binding]]
[[Category: Lee S]]
[[Category: Dna polymerase fold]]
[[Category: Min K]]
[[Category: Lyase-dna complex]]
[[Category: Monzingo AF]]
[[Category: Nucleolus]]
[[Category: Nucleotidyl transfer]]
[[Category: Transferase]]

Latest revision as of 12:36, 1 March 2024

DNA polymerase beta with O6mG in the template base opposite to incoming non-hydrolyzable CTP with manganese in the active site

4ny8, resolution 2.25Å

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