2HIK

heterotrimeric PCNA sliding clamp

2HIK の概要

• エントリーDOI: 10.2210/pdb2hik/pdb
• 関連するPDBエントリー: 2HII 2HIV 2HIX
• 分子名称: PCNA1 (SSO0397), PCNA2 (SSO1047), PCNA3 (SSO0405) (3 entities in total)
• 機能のキーワード: pcna sliding clamp, processivity factor, dna replication, heterotrimer, replication
• 由来する生物種: Sulfolobus solfataricus; 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 256378.33

構造登録者

Pascal, J.M.,Tsodikov, O.V.,Ellenberger, T. (登録日: 2006-06-29, 公開日: 2006-11-07, 最終更新日: 2024-11-20)

主引用文献

Pascal, J.M.,Tsodikov, O.V.,Hura, G.L.,Song, W.,Cotner, E.A.,Classen, S.,Tomkinson, A.E.,Tainer, J.A.,Ellenberger, T.
A Flexible Interface between DNA Ligase and PCNA Supports Conformational Switching and Efficient Ligation of DNA.
Mol.Cell, 24:279-291, 2006

PubMed Abstract: DNA sliding clamps encircle DNA and provide binding sites for many DNA-processing enzymes. However, it is largely unknown how sliding clamps like proliferating cell nuclear antigen (PCNA) coordinate multistep DNA transactions. We have determined structures of Sulfolobus solfataricus DNA ligase and heterotrimeric PCNA separately by X-ray diffraction and in complex by small-angle X-ray scattering (SAXS). Three distinct PCNA subunits assemble into a protein ring resembling the homotrimeric PCNA of humans but with three unique protein-binding sites. In the absence of nicked DNA, the Sulfolobus solfataricus DNA ligase has an open, extended conformation. When complexed with heterotrimeric PCNA, the DNA ligase binds to the PCNA3 subunit and ligase retains an open, extended conformation. A closed, ring-shaped conformation of ligase catalyzes a DNA end-joining reaction that is strongly stimulated by PCNA. This open-to-closed switch in the conformation of DNA ligase is accommodated by a malleable interface with PCNA that serves as an efficient platform for DNA ligation.

PubMed: 17052461
DOI: 10.1016/j.molcel.2006.08.015

実験手法

X-RAY DIFFRACTION (3.3 Å)