3FLO

Crystal structure of the carboxyl-terminal domain of yeast DNA polymerase alpha in complex with its B subunit

3FLO の概要

• エントリーDOI: 10.2210/pdb3flo/pdb
• 分子名称: DNA polymerase alpha subunit B, DNA polymerase alpha catalytic subunit A, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: protein-protein complex, phosphoesterase fold, ob fold, zinc-binding motif, dna replication, nucleus, phosphoprotein, dna-binding, dna-directed dna polymerase, nucleotidyltransferase, transferase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Nucleus: P38121 P13382
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 311633.59

構造登録者

Klinge, S.N.,Pellegrini, L. (登録日: 2008-12-19, 公開日: 2009-06-09, 最終更新日: 2024-03-20)

主引用文献

Klinge, S.,Nunez-Ramirez, R.,Llorca, O.,Pellegrini, L.
3D architecture of DNA Pol alpha reveals the functional core of multi-subunit replicative polymerases
Embo J., 28:1978-1987, 2009

PubMed Abstract: Eukaryotic DNA replication requires the coordinated activity of the multi-subunit DNA polymerases: Pol alpha, Pol delta and Pol epsilon. The conserved catalytic and regulatory B subunits associate in a constitutive heterodimer that represents the functional core of all three replicative polymerases. Here, we combine X-ray crystallography and electron microscopy (EM) to describe subunit interaction and 3D architecture of heterodimeric yeast Pol alpha. The crystal structure of the C-terminal domain (CTD) of the catalytic subunit bound to the B subunit illustrates a conserved mechanism of accessory factor recruitment by replicative polymerases. The EM reconstructions of Pol alpha reveal a bilobal shape with separate catalytic and regulatory modules. Docking of the B-CTD complex in the EM reconstruction shows that the B subunit is tethered to the polymerase domain through a structured but flexible linker. Our combined findings provide a structural template for the common functional architecture of the three major replicative DNA polymerases.

PubMed: 19494830
DOI: 10.1038/emboj.2009.150

実験手法

X-RAY DIFFRACTION (2.5 Å)