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4mf2

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{{STRUCTURE_4mf2| PDB=4mf2 | SCENE= }}
 
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===Structure of human DNA polymerase beta complexed with O6MG as the template base in a 1-nucleotide gapped DNA===
 
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{{ABSTRACT_PUBMED_24694247}}
 
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==Function==
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==Structure of human DNA polymerase beta complexed with O6MG as the template base in a 1-nucleotide gapped DNA==
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[[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>
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<StructureSection load='4mf2' size='340' side='right'caption='[[4mf2]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4mf2]] 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=4MF2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MF2 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6OG:6-O-METHYL+GUANOSINE-5-MONOPHOSPHATE'>6OG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mf2 OCA], [https://pdbe.org/4mf2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mf2 RCSB], [https://www.ebi.ac.uk/pdbsum/4mf2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mf2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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==About this Structure==
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==See Also==
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[[4mf2]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MF2 OCA].
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*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:024694247</ref><references group="xtra"/><references/>
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__TOC__
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[[Category: Koag, M C.]]
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</StructureSection>
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[[Category: Lee, S.]]
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[[Category: Homo sapiens]]
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[[Category: Min, K.]]
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[[Category: Large Structures]]
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[[Category: Monzingo, A F.]]
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[[Category: Koag MC]]
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[[Category: Dna polymerase]]
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[[Category: Lee S]]
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[[Category: Polymerase x family]]
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[[Category: Min K]]
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[[Category: Protein-dna complex]]
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[[Category: Monzingo AF]]
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[[Category: Transferase-dna complex]]
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Current revision

Structure of human DNA polymerase beta complexed with O6MG as the template base in a 1-nucleotide gapped DNA

PDB ID 4mf2

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