6l84

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'''Unreleased structure'''
 
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The entry 6l84 is ON HOLD
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==Complex of DNA polymerase IV and D-DNA duplex==
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<StructureSection load='6l84' size='340' side='right'caption='[[6l84]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6l84]] is a 3 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=6L84 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L84 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.602&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6l84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l84 OCA], [https://pdbe.org/6l84 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l84 RCSB], [https://www.ebi.ac.uk/pdbsum/6l84 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l84 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6l84" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharolobus solfataricus P2]]
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[[Category: Synthetic construct]]
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[[Category: An J]]
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[[Category: Chung HS]]
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[[Category: Hwang D]]

Current revision

Complex of DNA polymerase IV and D-DNA duplex

PDB ID 6l84

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