5FKU

cryo-EM structure of the E. coli replicative DNA polymerase complex in DNA free state (DNA polymerase III alpha, beta, epsilon, tau complex)

5FKU の概要

• エントリーDOI: 10.2210/pdb5fku/pdb
• 関連するPDBエントリー: 5FKV 5FKW
• EMDBエントリー: 3201
• 分子名称: DNA POLYMERASE III SUBUNIT ALPHA, DNA POLYMERASE III SUBUNIT BETA, DNA POLYMERASE III SUBUNIT EPSILON, ... (4 entities in total)
• 機能のキーワード: transferase, dna replication, dna polymerase iii alpha, dna polymerase iii beta, dna polymerase iii epsilon, dna polymerase iii tau
• 由来する生物種: ESCHERICHIA COLI K-12; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 254752.70

構造登録者

Fernandez-Leiro, R.,Conrad, J.,Scheres, S.H.W.,Lamers, M.H. (登録日: 2015-10-20, 公開日: 2015-11-25, 最終更新日: 2024-05-08)

主引用文献

Fernandez-Leiro, R.,Conrad, J.,Scheres, S.H.,Lamers, M.H.
cryo-EM structures of theE. colireplicative DNA polymerase reveal its dynamic interactions with the DNA sliding clamp, exonuclease andtau.
Elife, 4:-, 2015

PubMed Abstract: The replicative DNA polymerase PolIIIα from is a uniquely fast and processive enzyme. For its activity it relies on the DNA sliding clamp β, the proofreading exonuclease ε and the C-terminal domain of the clamp loader subunit τ. Due to the dynamic nature of the four-protein complex it has long been refractory to structural characterization. Here we present the 8 Å resolution cryo-electron microscopy structures of DNA-bound and DNA-free states of the PolIII-clamp-exonuclease-τ complex. The structures show how the polymerase is tethered to the DNA through multiple contacts with the clamp and exonuclease. A novel contact between the polymerase and clamp is made in the DNA bound state, facilitated by a large movement of the polymerase tail domain and τ. These structures provide crucial insights into the organization of the catalytic core of the replisome and form an important step towards determining the structure of the complete holoenzyme.

PubMed: 26499492
DOI: 10.7554/eLife.11134

実験手法

ELECTRON MICROSCOPY (8.34 Å)