3B39

Structure of the DnaG primase catalytic domain bound to ssDNA

3B39 の概要

• エントリーDOI: 10.2210/pdb3b39/pdb
• 関連するPDBエントリー: 1DD9 1DDE 1EQN
• 分子名称: DNA (5'-D(*DCP*DAP*DAP*DAP*DGP*DCP*DCP*DAP*DAP*DAP*DAP*DGP*DGP*DAP*DC)-3'), DNA primase (3 entities in total)
• 機能のキーワード: protein-dna complex, toprim fold, dna replication, dna-directed rna polymerase, metal-binding, nucleotidyltransferase, primosome, transcription, transferase, zinc-finger, transferase-dna complex, transferase/dna
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 81788.02

構造登録者

Corn, J.E.,Pelton, J.G.,Berger, J.M. (登録日: 2007-10-19, 公開日: 2008-01-15, 最終更新日: 2023-08-30)

主引用文献

Corn, J.E.,Pelton, J.G.,Berger, J.M.
Identification of a DNA primase template tracking site redefines the geometry of primer synthesis.
Nat.Struct.Mol.Biol., 15:163-169, 2008

PubMed Abstract: Primases are essential RNA polymerases required for the initiation of DNA replication, lagging strand synthesis and replication restart. Many aspects of primase function remain unclear, including how the enzyme associates with a moving nucleic acid strand emanating from a helicase and orients primers for handoff to replisomal components. Using a new screening method to trap transient macromolecular interactions, we determined the structure of the Escherichia coli DnaG primase catalytic domain bound to single-stranded DNA. The structure reveals an unanticipated binding site that engages nucleic acid in two distinct configurations, indicating that it serves as a nonspecific capture and tracking locus for template DNA. Bioinformatic and biochemical analyses show that this evolutionarily constrained region enforces template polarity near the active site and is required for primase function. Together, our findings reverse previous proposals for primer-template orientation and reconcile disparate studies to re-evaluate replication fork organization.

PubMed: 18193061
DOI: 10.1038/nsmb.1373

実験手法

X-RAY DIFFRACTION (2.35 Å)