Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6CX2

S177G Mutant of Yeast PCNA

Summary for 6CX2
Entry DOI10.2210/pdb6cx2/pdb
DescriptorProliferating cell nuclear antigen (1 entity in total)
Functional Keywordsdna replication, dna repair, dna recombination, scaffold, dna binding protein
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Total number of polymer chains1
Total formula weight29052.17
Authors
Powers, K.T. (deposition date: 2018-04-02, release date: 2018-04-11, Last modification date: 2023-10-04)
Primary citationKondratick, C.M.,Boehm, E.M.,Dieckman, L.M.,Powers, K.T.,Sanchez, J.C.,Mueting, S.R.,Washington, M.T.
Identification of New Mutations at the PCNA Subunit Interface that Block Translesion Synthesis.
PLoS ONE, 11:e0157023-, 2016
Cited by
PubMed Abstract: Proliferating 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.
PubMed: 27258147
DOI: 10.1371/journal.pone.0157023
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.101 Å)
Structure validation

242500

数据于2025-10-01公开中

PDB statisticsPDBj update infoContact PDBjnumon