6nkr
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Ternary complex crystal structure of K289M variant of DNA polymerase Beta with dGTP== | |
| - | + | <StructureSection load='6nkr' size='340' side='right'caption='[[6nkr]], [[Resolution|resolution]] 2.45Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6nkr]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NKR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NKR 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>, <scene name='pdbligand=DGT:2-DEOXYGUANOSINE-5-TRIPHOSPHATE'>DGT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |
| - | [[Category: | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOC:2,3-DIDEOXYCYTIDINE-5-MONOPHOSPHATE'>DOC</scene></td></tr> |
| - | [[Category: Wilson, S | + | <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=6nkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nkr OCA], [http://pdbe.org/6nkr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nkr RCSB], [http://www.ebi.ac.uk/pdbsum/6nkr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nkr ProSAT]</span></td></tr> |
| - | [[Category: | + | </table> |
| + | == Function == | ||
| + | [[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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Batra, V K]] | ||
| + | [[Category: Wilson, S H]] | ||
| + | [[Category: Conformational change]] | ||
| + | [[Category: Dna polymerase beta]] | ||
| + | [[Category: Enzyme mechanism]] | ||
| + | [[Category: K289m]] | ||
| + | [[Category: Lfer]] | ||
| + | [[Category: Transcription]] | ||
| + | [[Category: Transcription-dna complex]] | ||
Revision as of 07:34, 8 January 2020
Ternary complex crystal structure of K289M variant of DNA polymerase Beta with dGTP
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