4FYD

Crystal structure of yeast DNA polymerase alpha bound to DNA/RNA and dGTP

4FYD の概要

• エントリーDOI: 10.2210/pdb4fyd/pdb
• 関連するPDBエントリー: 4B08 4FVM 4FXD
• 分子名称: DNA polymerase alpha catalytic subunit A, DNA (5'-D(*TP*GP*AP*GP*CP*GP*TP*G*TP*GP*TP*AP*CP*CP*CP*CP*TP*GP*CP*CP*CP*GP*CP*CP*G)-3'), DNA/RNA (5'-R(*CP*GP*GP*CP*GP*GP*GP*CP*AP*G)-D(P*GP*G)-3'), ... (4 entities in total)
• 機能のキーワード: dna polymerase, dna replication, transferase-dna complex, transferase/dna
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Nucleus: P13382
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 230932.41

構造登録者

Perera, R.L.,Pellegrini, L. (登録日: 2012-07-04, 公開日: 2013-02-27, 最終更新日: 2023-09-13)

主引用文献

Perera, R.L.,Torella, R.,Klinge, S.,Kilkenny, M.L.,Maman, J.D.,Pellegrini, L.
Mechanism for priming DNA synthesis by yeast DNA Polymerase alpha
eLife, 2:e00482-, 2013

PubMed Abstract: The DNA Polymerase α (Pol α)/primase complex initiates DNA synthesis in eukaryotic replication. In the complex, Pol α and primase cooperate in the production of RNA-DNA oligonucleotides that prime synthesis of new DNA. Here we report crystal structures of the catalytic core of yeast Pol α in unliganded form, bound to an RNA primer/DNA template and extending an RNA primer with deoxynucleotides. We combine the structural analysis with biochemical and computational data to demonstrate that Pol α specifically recognizes the A-form RNA/DNA helix and that the ensuing synthesis of B-form DNA terminates primer synthesis. The spontaneous release of the completed RNA-DNA primer by the Pol α/primase complex simplifies current models of primer transfer to leading- and lagging strand polymerases. The proposed mechanism of nucleotide polymerization by Pol α might contribute to genomic stability by limiting the amount of inaccurate DNA to be corrected at the start of each Okazaki fragment. DOI:http://dx.doi.org/10.7554/eLife.00482.001.

PubMed: 23599895
DOI: 10.7554/eLife.00482

実験手法

X-RAY DIFFRACTION (3.1 Å)