2AU3

Crystal Structure of the Aquifex aeolicus primase (Zinc Binding and RNA Polymerase Domains)

2AU3 の概要

• エントリーDOI: 10.2210/pdb2au3/pdb
• 分子名称: DNA primase, ZINC ION (3 entities in total)
• 機能のキーワード: zinc ribbon, toprim, rna polymerase, dna replication, transferase
• 由来する生物種: Aquifex aeolicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46756.92

構造登録者

Corn, J.E.,Pease, P.J.,Hura, G.L.,Berger, J.M. (登録日: 2005-08-26, 公開日: 2005-11-15, 最終更新日: 2024-04-03)

主引用文献

Corn, J.E.,Pease, P.J.,Hura, G.L.,Berger, J.M.
Crosstalk between primase subunits can act to regulate primer synthesis in trans.
Mol.Cell, 20:391-401, 2005

PubMed Abstract: The coordination of primase function within the replisome is an essential but poorly understood feature of lagging strand synthesis. By using crystallography and small-angle X-ray scattering (SAXS), we show that functional elements of bacterial primase transition between two dominant conformations: an extended form that uncouples a regulatory domain from its associated RNA polymerase core and a compact state that sequesters the regulatory region from the site of primer synthesis. FRET studies and priming assays reveal that the regulatory domain of one primase subunit productively associates with nucleic acid that is bound to the polymerase domain of a second protomer in trans. This intersubunit interaction allows primase to select initiation sites on template DNA and implicates the regulatory domain as a "molecular brake" that restricts primer length. Our data suggest that the replisome may cooperatively use multiple primases and this conformational switch to control initiation frequency, processivity, and ultimately, Okazaki fragment synthesis.

PubMed: 16285921
DOI: 10.1016/j.molcel.2005.09.004

実験手法

X-RAY DIFFRACTION (2 Å)