3CQ8

Ternary complex of the L415F mutant RB69 exo(-)polymerase

3CQ8 の概要

• エントリーDOI: 10.2210/pdb3cq8/pdb
• 関連するPDBエントリー: 1IG9 2OZS
• 分子名称: DNA (5'-D(*DAP*DCP*DAP*DGP*DGP*DTP*DAP*DAP*DGP*DCP*DAP*DGP*DTP*DCP*DCP*DGP*DCP*DG)-3'), DNA (5'-D(*DGP*DCP*DGP*DGP*DAP*DCP*DTP*DGP*DCP*DTP*DTP*DAP*DCP*DC)-3'), DNA polymerase, ... (8 entities in total)
• 機能のキーワード: b family polymerase fold, dna replication, dna-binding, dna-directed dna polymerase, exonuclease, hydrolase, nuclease, nucleotidyltransferase, transferase, transferase-dna complex, transferase/dna
• 由来する生物種: Enterobacteria phage
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 115564.42

構造登録者

Zhong, X.,Pedersen, L.C.,Kunkel, T.A. (登録日: 2008-04-02, 公開日: 2008-09-02, 最終更新日: 2023-08-30)

主引用文献

Zhong, X.,Pedersen, L.C.,Kunkel, T.A.
Characterization of a replicative DNA polymerase mutant with reduced fidelity and increased translesion synthesis capacity.
Nucleic Acids Res., 36:3892-3904, 2008

PubMed Abstract: Changing a highly conserved amino acid in motif A of any of the four yeast family B DNA polymerases, DNA polymerase alpha, delta, epsilon or zeta, results in yeast strains with elevated mutation rates. In order to better understand this phenotype, we have performed structure-function studies of homologous mutants of RB69 DNA polymerase (RB69 pol), a structural model for family B members. When Leu415 in RB69 pol is replaced with phenylalanine or glycine, the mutant polymerases retain high-catalytic efficiency for correct nucleotide incorporation, yet have increased error rates due to increased misinsertion, increased mismatch extension and inefficient proofreading. The Leu415Phe mutant also has increased dNTP insertion efficiency opposite a template 8-oxoG and opposite an abasic site. The 2.5 A crystal structure of a ternary complex of RB69 L415F pol with a correctly base-paired incoming dTTP reveals that the phenylalanine ring is accommodated within a cavity seen in the wild-type enzyme, without steric clash or major change in active site geometry, consistent with retention of high-catalytic efficiency for correct incorporation. In addition, slight structural differences were observed that could be relevant to the reduced fidelity of L415F RB69 pol.

PubMed: 18503083
DOI: 10.1093/nar/gkn312

実験手法

X-RAY DIFFRACTION (2.5 Å)