1ZT2

Heterodimeric structure of the core primase.

1ZT2 の概要

• エントリーDOI: 10.2210/pdb1zt2/pdb
• 分子名称: DNA primase small subunit, DNA primase large subunit, ZINC ION, ... (5 entities in total)
• 機能のキーワード: heterodimeric complex, replication, transferase
• 由来する生物種: Sulfolobus solfataricus; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 128977.56

構造登録者

Lao-Sirieix, S.H.,Nookala, R.K.,Roversi, P.,Bell, S.D.,Pellegrini, L. (登録日: 2005-05-26, 公開日: 2005-11-08, 最終更新日: 2024-11-20)

主引用文献

Lao-Sirieix, S.H.,Nookala, R.K.,Roversi, P.,Bell, S.D.,Pellegrini, L.
Structure of the heterodimeric core primase.
Nat.Struct.Mol.Biol., 12:1137-1144, 2005

PubMed Abstract: Primases are DNA-dependent RNA polymerases that synthesize the oligoribonucleotide primers essential to DNA replication. In archaeal and eukaryotic organisms, the core primase is a heterodimeric enzyme composed of a small and a large subunit. Here we report a crystallographic and biochemical analysis of the core primase from the archaeon Sulfolobus solfataricus. The structure provides the first three-dimensional description of the large subunit and its interaction with the small subunit. The evolutionary conservation of amino acids at the protein-protein interface implies that the observed mode of subunit association is conserved among archaeal and eukaryotic primases. The orientation of the large subunit in the core primase probably excludes its direct involvement in catalysis. Modeling of a DNA-RNA helix together with structure-based site-directed mutagenesis provides insight into the mechanism of template DNA binding and RNA primer synthesis.

PubMed: 16273105
DOI: 10.1038/nsmb1013

実験手法

X-RAY DIFFRACTION (3.33 Å)