1DD9

STRUCTURE OF THE DNAG CATALYTIC CORE

1DD9 の概要

• エントリーDOI: 10.2210/pdb1dd9/pdb
• 関連するPDBエントリー: 1DDE
• 分子名称: DNA PRIMASE, STRONTIUM ION (3 entities in total)
• 機能のキーワード: toprim, 3-helix bundle, dna-binding protein, rna polymerase, replication protein, primase, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38309.87

構造登録者

Keck, J.L.,Roche, D.D.,Lynch, A.S.,Berger, J.M. (登録日: 1999-11-09, 公開日: 2000-04-07, 最終更新日: 2024-02-07)

主引用文献

Keck, J.L.,Roche, D.D.,Lynch, A.S.,Berger, J.M.
Structure of the RNA polymerase domain of E. coli primase.
Science, 287:2482-2486, 2000

PubMed Abstract: All cellular organisms use specialized RNA polymerases called "primases" to synthesize RNA primers for the initiation of DNA replication. The high-resolution crystal structure of a primase, comprising the catalytic core of the Escherichia coli DnaG protein, was determined. The core structure contains an active-site architecture that is unrelated to other DNA or RNA polymerase palm folds, but is instead related to the "toprim" fold. On the basis of the structure, it is likely that DnaG binds nucleic acid in a groove clustered with invariant residues and that DnaG is positioned within the replisome to accept single-stranded DNA directly from the replicative helicase.

PubMed: 10741967
DOI: 10.1126/science.287.5462.2482

実験手法

X-RAY DIFFRACTION (1.6 Å)