6cx2: Difference between revisions
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==S177G Mutant of Yeast PCNA== | ==S177G Mutant of Yeast PCNA== | ||
<StructureSection load='6cx2' size='340' side='right' caption='[[6cx2]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='6cx2' size='340' side='right'caption='[[6cx2]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6cx2]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6cx2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CX2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CX2 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]] 3.101Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6cx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cx2 OCA], [https://pdbe.org/6cx2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cx2 RCSB], [https://www.ebi.ac.uk/pdbsum/6cx2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cx2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PCNA_YEAST PCNA_YEAST] This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair.<ref>PMID:11545742</ref> <ref>PMID:12226657</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 20: | ||
==See Also== | ==See Also== | ||
*[[Proliferating | *[[Proliferating cell nuclear antigen 3D structures|Proliferating cell nuclear antigen 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae S288C]] | ||
[[Category: | [[Category: Powers KT]] | ||
Latest revision as of 18:12, 4 October 2023
S177G Mutant of Yeast PCNAS177G Mutant of Yeast PCNA
Structural highlights
FunctionPCNA_YEAST This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair.[1] [2] Publication Abstract from PubMedProliferating cell nuclear antigen (PCNA) plays an essential role in DNA replication and repair by interacting with a large number of proteins involved in these processes. Two amino acid substitutions in PCNA, both located at the subunit interface, have previously been shown to block translesion synthesis (TLS), a pathway for bypassing DNA damage during replication. To better understand the role of the subunit interface in TLS, we used random mutagenesis to generate a set of 33 PCNA mutants with substitutions at the subunit interface. We assayed the full set of mutants for viability and sensitivity to ultraviolet (UV) radiation. We then selected a subset of 17 mutants and measured their rates of cell growth, spontaneous mutagenesis, and UV-induced mutagenesis. All except three of these 17 mutants were partially or completely defective in induced mutagenesis, which indicates a partial or complete loss of TLS. These results demonstrate that the integrity of the subunit interface of PCNA is essential for efficient TLS and that even conservative substitutions have the potential to disrupt this process. Identification of New Mutations at the PCNA Subunit Interface that Block Translesion Synthesis.,Kondratick CM, Boehm EM, Dieckman LM, Powers KT, Sanchez JC, Mueting SR, Washington MT PLoS One. 2016 Jun 3;11(6):e0157023. doi: 10.1371/journal.pone.0157023., eCollection 2016. PMID:27258147[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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