3khh
From Proteopedia
(Difference between revisions)
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==Dpo4 extension ternary complex with a C base opposite the 2-aminofluorene-guanine [AF]G lesion== | ==Dpo4 extension ternary complex with a C base opposite the 2-aminofluorene-guanine [AF]G lesion== | ||
- | <StructureSection load='3khh' size='340' side='right' caption='[[3khh]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='3khh' size='340' side='right'caption='[[3khh]], [[Resolution|resolution]] 2.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3khh]] is a 6 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3khh]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Sacs2 Sacs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KHH FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AF:2-AMINOFLUORENE'>AF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DGT:2-DEOXYGUANOSINE-5-TRIPHOSPHATE'>DGT</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AF:2-AMINOFLUORENE'>AF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DGT:2-DEOXYGUANOSINE-5-TRIPHOSPHATE'>DGT</scene></td></tr> |
<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> | <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> | ||
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3khg|3khg]], [[3khl|3khl]], [[3khr|3khr]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3khg|3khg]], [[3khl|3khl]], [[3khr|3khr]]</div></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dbh, dpo4, SSO2448 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dbh, dpo4, SSO2448 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SACS2])</td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3khh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3khh OCA], [https://pdbe.org/3khh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3khh RCSB], [https://www.ebi.ac.uk/pdbsum/3khh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3khh ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/DPO4_SULSO DPO4_SULSO]] Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. It is involved in translesional synthesis.[HAMAP-Rule:MF_01113] |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</div> | </div> | ||
<div class="pdbe-citations 3khh" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3khh" style="background-color:#fffaf0;"></div> | ||
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- | ==See Also== | ||
- | *[[DNA polymerase|DNA polymerase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: DNA-directed DNA polymerase]] | [[Category: DNA-directed DNA polymerase]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Sacs2]] | [[Category: Sacs2]] | ||
[[Category: Malinina, L]] | [[Category: Malinina, L]] |
Revision as of 12:25, 13 October 2021
Dpo4 extension ternary complex with a C base opposite the 2-aminofluorene-guanine [AF]G lesion
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Categories: DNA-directed DNA polymerase | Large Structures | Sacs2 | Malinina, L | Patel, D J | Rechkoblit, O | 2-aminofluorene | Dna damage | Dna polymerase | Dna repair | Dna replication | Dna-binding | Dna-directed dna polymerase | Lesion bypass | Magnesium | Metal-binding | Mutator protein | Nucleotidyltransferase | Semi-targeted mutagenesis | Transferase | Transferase-dna complex | Y-family polymerase