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==BINARY COMPLEX OF SULFOLOBUS SOLFATARICUS DPO4 DNA POLYMERASE AND 1, N2-ETHENOGUANINE MODIFIED DNA, MAGNESIUM FORM==
==BINARY COMPLEX OF SULFOLOBUS SOLFATARICUS DPO4 DNA POLYMERASE AND 1, N2-ETHENOGUANINE MODIFIED DNA, MAGNESIUM FORM==
<StructureSection load='2xc9' size='340' side='right' caption='[[2xc9]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='2xc9' size='340' side='right'caption='[[2xc9]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2xc9]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulso Sulso]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XC9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XC9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2xc9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulso Sulso]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XC9 FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNE:1,N2-ETHENOGUANINE'>GNE</scene></td></tr>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNE:1,N2-ETHENOGUANINE'>GNE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2asl|2asl]], [[1s0m|1s0m]], [[2jeg|2jeg]], [[1rys|1rys]], [[2v4s|2v4s]], [[2j6t|2j6t]], [[2w9b|2w9b]], [[1n56|1n56]], [[1jx4|1jx4]], [[2atl|2atl]], [[2c22|2c22]], [[2va2|2va2]], [[1s97|1s97]], [[2agq|2agq]], [[2jej|2jej]], [[2w9c|2w9c]], [[2asj|2asj]], [[2ago|2ago]], [[2w9a|2w9a]], [[2asd|2asd]], [[1jxl|1jxl]], [[1n48|1n48]], [[2bq3|2bq3]], [[2uvu|2uvu]], [[2j6u|2j6u]], [[2agp|2agp]], [[2c2r|2c2r]], [[1s0n|1s0n]], [[1s0o|1s0o]], [[2jef|2jef]], [[2w8l|2w8l]], [[2uvw|2uvw]], [[2bqr|2bqr]], [[2jei|2jei]], [[1s9f|1s9f]], [[2au0|2au0]], [[2bqu|2bqu]], [[2c28|2c28]], [[2v9w|2v9w]], [[2v4r|2v4r]], [[2c2e|2c2e]], [[1ryr|1ryr]], [[2uvv|2uvv]], [[2c2d|2c2d]], [[2v4q|2v4q]], [[2br0|2br0]], [[1s10|1s10]], [[2j6s|2j6s]], [[2uvr|2uvr]], [[2va3|2va3]], [[2w8k|2w8k]], [[2v4t|2v4t]], [[2xca|2xca]], [[2xcp|2xcp]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2asl|2asl]], [[1s0m|1s0m]], [[2jeg|2jeg]], [[1rys|1rys]], [[2v4s|2v4s]], [[2j6t|2j6t]], [[2w9b|2w9b]], [[1n56|1n56]], [[1jx4|1jx4]], [[2atl|2atl]], [[2c22|2c22]], [[2va2|2va2]], [[1s97|1s97]], [[2agq|2agq]], [[2jej|2jej]], [[2w9c|2w9c]], [[2asj|2asj]], [[2ago|2ago]], [[2w9a|2w9a]], [[2asd|2asd]], [[1jxl|1jxl]], [[1n48|1n48]], [[2bq3|2bq3]], [[2uvu|2uvu]], [[2j6u|2j6u]], [[2agp|2agp]], [[2c2r|2c2r]], [[1s0n|1s0n]], [[1s0o|1s0o]], [[2jef|2jef]], [[2w8l|2w8l]], [[2uvw|2uvw]], [[2bqr|2bqr]], [[2jei|2jei]], [[1s9f|1s9f]], [[2au0|2au0]], [[2bqu|2bqu]], [[2c28|2c28]], [[2v9w|2v9w]], [[2v4r|2v4r]], [[2c2e|2c2e]], [[1ryr|1ryr]], [[2uvv|2uvv]], [[2c2d|2c2d]], [[2v4q|2v4q]], [[2br0|2br0]], [[1s10|1s10]], [[2j6s|2j6s]], [[2uvr|2uvr]], [[2va3|2va3]], [[2w8k|2w8k]], [[2v4t|2v4t]], [[2xca|2xca]], [[2xcp|2xcp]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DPO4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DPO4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span></td></tr>
<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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xc9 OCA], [http://pdbe.org/2xc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xc9 RCSB], [http://www.ebi.ac.uk/pdbsum/2xc9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xc9 ProSAT]</span></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=2xc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xc9 OCA], [https://pdbe.org/2xc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xc9 RCSB], [https://www.ebi.ac.uk/pdbsum/2xc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xc9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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]  
[[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 2xc9" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 2xc9" style="background-color:#fffaf0;"></div>
==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: Sulso]]
[[Category: Sulso]]
[[Category: Egli, M]]
[[Category: Egli, M]]

Revision as of 11:38, 10 November 2021

BINARY COMPLEX OF SULFOLOBUS SOLFATARICUS DPO4 DNA POLYMERASE AND 1, N2-ETHENOGUANINE MODIFIED DNA, MAGNESIUM FORMBINARY COMPLEX OF SULFOLOBUS SOLFATARICUS DPO4 DNA POLYMERASE AND 1, N2-ETHENOGUANINE MODIFIED DNA, MAGNESIUM FORM

Structural highlights

2xc9 is a 3 chain structure with sequence from Sulso. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:DPO4 (SULSO)
Activity:DNA-directed DNA polymerase, with EC number 2.7.7.7
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Crystal structures of a binary Mg2+-form Dpo4-DNA complex with 1,N2-etheno-dG in the template strand as well as of ternary Mg2+-form Dpo4-DNA-dCTP/dGTP complexes with 8-oxoG in the template strand have been determined. Comparison of their conformations and active-site geometries with those of the corresponding Ca2+-form complexes revealed that the DNA and polymerase undergo subtle changes as a result of the catalytically more active Mg2+ occupying both the A and B sites.

Metal-ion dependence of the active-site conformation of the translesion DNA polymerase Dpo4 from Sulfolobus solfataricus.,Irimia A, Loukachevitch LV, Eoff RL, Guengerich FP, Egli M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Sep 1;66(Pt, 9):1013-8. Epub 2010 Aug 21. PMID:20823515[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Irimia A, Loukachevitch LV, Eoff RL, Guengerich FP, Egli M. Metal-ion dependence of the active-site conformation of the translesion DNA polymerase Dpo4 from Sulfolobus solfataricus. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Sep 1;66(Pt, 9):1013-8. Epub 2010 Aug 21. PMID:20823515 doi:10.1107/S1744309110029374

2xc9, resolution 2.20Å

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