5F0Q

Crystal structure of C-terminal domain of the human DNA primase large subunit with bound DNA template/RNA primer

5F0Q の概要

• エントリーDOI: 10.2210/pdb5f0q/pdb
• 関連するPDBエントリー: 5F0S
• 分子名称: DNA primase large subunit, RNA (5'-R(P*GP*GP*CP*GP*GP*C)-3'), DNA (5'-D(*GP*CP*CP*GP*CP*CP*AP*AP*CP*AP*TP*A)-3'), ... (6 entities in total)
• 機能のキーワード: tranferase-dna-rna complex, dna primase, large subunit, iron-sulfur cluster, rna, dna, primer, template, triphosphate, initiation site, tranferase/dna/rna
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 56251.58

構造登録者

Tahirov, T.H.,Baranovskiy, A.G.,Babayeva, N.D. (登録日: 2015-11-28, 公開日: 2016-03-23, 最終更新日: 2023-09-27)

主引用文献

Baranovskiy, A.G.,Babayeva, N.D.,Zhang, Y.,Gu, J.,Suwa, Y.,Pavlov, Y.I.,Tahirov, T.H.
Mechanism of Concerted RNA-DNA Primer Synthesis by the Human Primosome.
J.Biol.Chem., 291:10006-10020, 2016

PubMed Abstract: The human primosome, a 340-kilodalton complex of primase and DNA polymerase α (Polα), synthesizes chimeric RNA-DNA primers to be extended by replicative DNA polymerases δ and ϵ. The intricate mechanism of concerted primer synthesis by two catalytic centers was an enigma for over three decades. Here we report the crystal structures of two key complexes, the human primosome and the C-terminal domain of the primase large subunit (p58C) with bound DNA/RNA duplex. These structures, along with analysis of primase/polymerase activities, provide a plausible mechanism for all transactions of the primosome including initiation, elongation, accurate counting of RNA primer length, primer transfer to Polα, and concerted autoregulation of alternate activation/inhibition of the catalytic centers. Our findings reveal a central role of p58C in the coordinated actions of two catalytic domains in the primosome and ultimately could impact the design of anticancer drugs.

PubMed: 26975377
DOI: 10.1074/jbc.M116.717405

実験手法

X-RAY DIFFRACTION (2.21 Å)