2xcp: Difference between revisions

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<StructureSection load='2xcp' size='340' side='right'caption='[[2xcp]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='2xcp' size='340' side='right'caption='[[2xcp]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2xcp]] is a 6 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=2XCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XCP FirstGlance]. <br>
<table><tr><td colspan='2'>[[2xcp]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XCP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCP:2-DEOXYCYTIDINE-5-TRIPHOSPHATE'>DCP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=8OG:8-OXO-2-DEOXY-GUANOSINE-5-MONOPHOSPHATE'>8OG</scene>, <scene name='pdbligand=DOC:2,3-DIDEOXYCYTIDINE-5-MONOPHOSPHATE'>DOC</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8OG:8-OXO-2-DEOXY-GUANOSINE-5-MONOPHOSPHATE'>8OG</scene>, <scene name='pdbligand=DCP:2-DEOXYCYTIDINE-5-TRIPHOSPHATE'>DCP</scene>, <scene name='pdbligand=DOC:2,3-DIDEOXYCYTIDINE-5-MONOPHOSPHATE'>DOC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1s0m|1s0m]], [[2asl|2asl]], [[2jeg|2jeg]], [[1rys|1rys]], [[2v4s|2v4s]], [[2j6t|2j6t]], [[2w9b|2w9b]], [[1n56|1n56]], [[2atl|2atl]], [[1jx4|1jx4]], [[2c22|2c22]], [[2va2|2va2]], [[1s97|1s97]], [[2agq|2agq]], [[2jej|2jej]], [[2w9c|2w9c]], [[2ago|2ago]], [[2asj|2asj]], [[2asd|2asd]], [[2w9a|2w9a]], [[1jxl|1jxl]], [[1n48|1n48]], [[2bq3|2bq3]], [[2j6u|2j6u]], [[2uvu|2uvu]], [[2agp|2agp]], [[2c2r|2c2r]], [[1s0n|1s0n]], [[2xc9|2xc9]], [[2jef|2jef]], [[1s0o|1s0o]], [[2w8l|2w8l]], [[2uvw|2uvw]], [[2bqr|2bqr]], [[2jei|2jei]], [[2au0|2au0]], [[1s9f|1s9f]], [[2bqu|2bqu]], [[2xca|2xca]], [[2c28|2c28]], [[2v9w|2v9w]], [[2v4r|2v4r]], [[2c2e|2c2e]], [[1ryr|1ryr]], [[2uvv|2uvv]], [[2c2d|2c2d]], [[2v4q|2v4q]], [[1s10|1s10]], [[2br0|2br0]], [[2j6s|2j6s]], [[2uvr|2uvr]], [[2va3|2va3]], [[2w8k|2w8k]], [[2v4t|2v4t]]</div></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'>[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'>[https://proteopedia.org/fgij/fg.htm?mol=2xcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xcp OCA], [https://pdbe.org/2xcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xcp RCSB], [https://www.ebi.ac.uk/pdbsum/2xcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xcp 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=2xcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xcp OCA], [https://pdbe.org/2xcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xcp RCSB], [https://www.ebi.ac.uk/pdbsum/2xcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xcp 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]
[https://www.uniprot.org/uniprot/DPO4_SACS2 DPO4_SACS2] 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.
== 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 2xcp" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 2xcp" style="background-color:#fffaf0;"></div>
==See Also==
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: DNA-directed DNA polymerase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sulso]]
[[Category: Saccharolobus solfataricus P2]]
[[Category: Egli, M]]
[[Category: Egli M]]
[[Category: Irimia, A]]
[[Category: Irimia A]]
[[Category: Dna-transferase complex]]
[[Category: Nucleotidyltransferase]]
[[Category: Transferase]]
[[Category: Translesion dna polymerase]]

Latest revision as of 13:28, 20 December 2023

TERNARY COMPLEX OF SULFOLOBUS SOLFATARICUS DPO4 DNA POLYMERASE, 7,8- DIHYDRO-8-OXODEOXYGUANINE MODIFIED DNA AND dCTP - MAGNESIUM FORMTERNARY COMPLEX OF SULFOLOBUS SOLFATARICUS DPO4 DNA POLYMERASE, 7,8- DIHYDRO-8-OXODEOXYGUANINE MODIFIED DNA AND dCTP - MAGNESIUM FORM

Structural highlights

2xcp is a 6 chain structure with sequence from Saccharolobus solfataricus P2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DPO4_SACS2 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.

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.

See Also

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

2xcp, resolution 2.60Å

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