1EQN

E.COLI PRIMASE CATALYTIC CORE

1EQN の概要

• エントリーDOI: 10.2210/pdb1eqn/pdb
• 分子名称: DNA PRIMASE (1 entity in total)
• 機能のキーワード: toprim domain, rossmann fold, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 183104.70

構造登録者

Podobnik, M.,McInerney, P.,O'Donnell, M.,Kuriyan, J. (登録日: 2000-04-05, 公開日: 2000-06-30, 最終更新日: 2024-11-06)

主引用文献

Podobnik, M.,McInerney, P.,O'Donnell, M.,Kuriyan, J.
A TOPRIM domain in the crystal structure of the catalytic core of Escherichia coli primase confirms a structural link to DNA topoisomerases.
J.Mol.Biol., 300:353-362, 2000

PubMed Abstract: Primases synthesize short RNA strands on single-stranded DNA templates, thereby generating the hybrid duplexes required for the initiation of synthesis by DNA polymerases. We present the crystal structure of the catalytic unit of a primase enzyme, that of a approximately 320 residue fragment of Escherichia coli primase, determined at 2.9 A resolution. Central to the catalytic unit is a TOPRIM domain that is strikingly similar in its structure to that of corresponding domains in DNA topoisomerases, but is unrelated to the catalytic centers of other DNA or RNA polymerases. The catalytic domain of primase is crescent-shaped, and the concave face of the crescent is predicted to accommodate about 10 base-pairs of RNA-DNA duplex in a loose interaction, thereby limiting processivity.

PubMed: 10873470
DOI: 10.1006/jmbi.2000.3844

実験手法

X-RAY DIFFRACTION (2.9 Å)