3maq: Difference between revisions
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<StructureSection load='3maq' size='340' side='right'caption='[[3maq]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='3maq' size='340' side='right'caption='[[3maq]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3maq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3maq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3k5a 3k5a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MAQ FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DGT:2-DEOXYGUANOSINE-5-TRIPHOSPHATE'>DGT</scene>, <scene name='pdbligand=DOC:2,3-DIDEOXYCYTIDINE-5-MONOPHOSPHATE'>DOC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3maq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3maq OCA], [https://pdbe.org/3maq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3maq RCSB], [https://www.ebi.ac.uk/pdbsum/3maq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3maq 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=3maq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3maq OCA], [https://pdbe.org/3maq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3maq RCSB], [https://www.ebi.ac.uk/pdbsum/3maq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3maq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/DPO2_ECOLI DPO2_ECOLI] Thought to be involved in DNA repair and/or mutagenesis. | |||
== 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 3maq" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3maq" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Wang | [[Category: Wang F]] | ||
[[Category: Yang | [[Category: Yang W]] | ||
Latest revision as of 11:50, 6 September 2023
Crystal structure of E.coli Pol II-normal DNA-dGTP ternary complexCrystal structure of E.coli Pol II-normal DNA-dGTP ternary complex
Structural highlights
FunctionDPO2_ECOLI Thought to be involved in DNA repair and/or mutagenesis. 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 PubMedE. coli DNA Pol II and eukaryotic Rev3 are B-family polymerases that can extend primers past a damaged or mismatched site when the high-fidelity replicative polymerases in the same family are ineffective. We report here the biochemical and structural properties of DNA Pol II that facilitate this translesion synthesis. DNA Pol II can extend primers past lesions either directly or by template skipping, in which small protein cavities outside of the active site accommodate looped-out template nucleotides 1 or 2 bp upstream. Because of multiple looping-out alternatives, mutation spectra of bypass synthesis are complicated. Moreover, translesion synthesis is enhanced by altered partitioning of DNA substrate between the polymerase active site and the proofreading exonuclease site. Compared to the replicative B family polymerases, DNA Pol II has subtle amino acid changes remote from the active site that allow it to replicate normal DNA with high efficiency yet conduct translesion synthesis when needed. Structural insight into translesion synthesis by DNA Pol II.,Wang F, Yang W Cell. 2009 Dec 24;139(7):1279-89. PMID:20064374[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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