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4mf2
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| - | {{STRUCTURE_4mf2| PDB=4mf2 | SCENE= }} | ||
| - | ===Structure of human DNA polymerase beta complexed with O6MG as the template base in a 1-nucleotide gapped DNA=== | ||
| - | {{ABSTRACT_PUBMED_24694247}} | ||
| - | == | + | ==Structure of human DNA polymerase beta complexed with O6MG as the template base in a 1-nucleotide gapped DNA== |
| - | [[http://www.uniprot.org/uniprot/DPOLB_HUMAN DPOLB_HUMAN | + | <StructureSection load='4mf2' size='340' side='right'caption='[[4mf2]], [[Resolution|resolution]] 2.40Å' scene=''> |
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
| + | <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> | ||
| + | <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> | ||
| + | </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> | ||
| - | == | + | ==See Also== |
| - | [[ | + | *[[DNA polymerase 3D structures|DNA polymerase 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Koag MC]] |
| - | [[Category: | + | [[Category: Lee S]] |
| - | [[Category: | + | [[Category: Min K]] |
| - | + | [[Category: Monzingo AF]] | |
| - | + | ||
Current revision
Structure of human DNA polymerase beta complexed with O6MG as the template base in a 1-nucleotide gapped DNA
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Categories: Homo sapiens | Large Structures | Koag MC | Lee S | Min K | Monzingo AF
