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==Complex of DNA polymerase IV and L-DNA duplex== | ==Complex of DNA polymerase IV and L-DNA duplex== | ||
<StructureSection load='6l97' size='340' side='right'caption='[[6l97]]' scene=''> | <StructureSection load='6l97' size='340' side='right'caption='[[6l97]], [[Resolution|resolution]] 2.36Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L97 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6l97]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L97 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L97 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.362Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0DA:2-DEOXY-L-RIBO-FURANOSYL+ADENOSINE-5-MONOPHOSPHATE'>0DA</scene>, <scene name='pdbligand=0DC:2-DEOXY-L-RIBO-FURANOSYL+CYTOSINE-5-MONOPHOSPHATE'>0DC</scene>, <scene name='pdbligand=0DG:2-DEOXY-L-RIBO-FURANOSYL+GUANINE-5-MONOPHOSPHATE'>0DG</scene>, <scene name='pdbligand=0DT:2-DEOXY-L-RIBO-FURANOSYL+THYMIDINE-5-MONOPHOSPHATE'>0DT</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=6l97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l97 OCA], [https://pdbe.org/6l97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l97 RCSB], [https://www.ebi.ac.uk/pdbsum/6l97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l97 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[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. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The intrinsic l-DNA binding properties of a natural DNA polymerase was discovered. The binding affinity of Dpo4 polymerase for l-DNA was comparable to that for d-DNA. The crystal structure of Dpo4/l-DNA complex revealed a dimer formed by the little finger domain that provides a binding site for l-DNA. | |||
The crystal structure of a natural DNA polymerase complexed with mirror DNA.,An J, Choi J, Hwang D, Park J, Pemble CW 4th, Duong THM, Kim KR, Ahn H, Chung HS, Ahn DR Chem Commun (Camb). 2020 Feb 18;56(14):2186-2189. doi: 10.1039/c9cc09351f. Epub, 2020 Jan 23. PMID:31971182<ref>PMID:31971182</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6l97" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Saccharolobus solfataricus P2]] | |||
[[Category: Synthetic construct]] | |||
[[Category: An J]] | [[Category: An J]] | ||
[[Category: Chung HS]] | [[Category: Chung HS]] | ||
[[Category: Hwang D]] | [[Category: Hwang D]] | ||
Latest revision as of 13:53, 22 November 2023
Complex of DNA polymerase IV and L-DNA duplexComplex of DNA polymerase IV and L-DNA duplex
Structural highlights
FunctionDPO4_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. Publication Abstract from PubMedThe intrinsic l-DNA binding properties of a natural DNA polymerase was discovered. The binding affinity of Dpo4 polymerase for l-DNA was comparable to that for d-DNA. The crystal structure of Dpo4/l-DNA complex revealed a dimer formed by the little finger domain that provides a binding site for l-DNA. The crystal structure of a natural DNA polymerase complexed with mirror DNA.,An J, Choi J, Hwang D, Park J, Pemble CW 4th, Duong THM, Kim KR, Ahn H, Chung HS, Ahn DR Chem Commun (Camb). 2020 Feb 18;56(14):2186-2189. doi: 10.1039/c9cc09351f. Epub, 2020 Jan 23. PMID:31971182[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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