3U60

Structure of T4 Bacteriophage Clamp Loader Bound To Open Clamp, DNA and ATP Analog

3U60 の概要

• エントリーDOI: 10.2210/pdb3u60/pdb
• 関連するPDBエントリー: 1CZD 1JR3 1SXJ 1XXH 3GLF 3U5Z 3U61
• 分子名称: DNA polymerase accessory protein 44, Template DNA strand, Primer DNA strand, ... (8 entities in total)
• 機能のキーワード: aaa+, atp hydrolase, sliding clamp, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Enterobacteria phage T4; 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 259944.82

構造登録者

Kelch, B.A.,Makino, D.L.,O'Donnell, M.,Kuriyan, J. (登録日: 2011-10-11, 公開日: 2012-01-04, 最終更新日: 2024-11-06)

主引用文献

Kelch, B.A.,Makino, D.L.,O'Donnell, M.,Kuriyan, J.
How a DNA polymerase clamp loader opens a sliding clamp.
Science, 334:1675-1680, 2011

PubMed Abstract: Processive chromosomal replication relies on sliding DNA clamps, which are loaded onto DNA by pentameric clamp loader complexes belonging to the AAA+ family of adenosine triphosphatases (ATPases). We present structures for the ATP-bound state of the clamp loader complex from bacteriophage T4, bound to an open clamp and primer-template DNA. The clamp loader traps a spiral conformation of the open clamp so that both the loader and the clamp match the helical symmetry of DNA. One structure reveals that ATP has been hydrolyzed in one subunit and suggests that clamp closure and ejection of the loader involves disruption of the ATP-dependent match in symmetry. The structures explain how synergy among the loader, the clamp, and DNA can trigger ATP hydrolysis and release of the closed clamp on DNA.

PubMed: 22194570
DOI: 10.1126/science.1211884

実験手法

X-RAY DIFFRACTION (3.34 Å)