1XO0

High resolution structure of the holliday junction intermediate in cre-loxp site-specific recombination

1XO0 の概要

• エントリーDOI: 10.2210/pdb1xo0/pdb
• 関連するPDBエントリー: 1XNS 2CRX 3CRX
• 分子名称: loxP, Recombinase CRE, ... (4 entities in total)
• 機能のキーワード: cre recombinase, holliday junction, recombination, complex (recombinase-dna), hydrolase, ligase-dna complex, ligase/dna
• 由来する生物種: Enterobacteria phage P1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 94618.61

構造登録者

Ghosh, K.,Lau, C.K.,Guo, F.,Segall, A.M.,Van Duyne, G.D. (登録日: 2004-10-05, 公開日: 2004-12-14, 最終更新日: 2023-08-23)

主引用文献

Ghosh, K.,Lau, C.K.,Guo, F.,Segall, A.M.,Van Duyne, G.D.
Peptide trapping of the Holliday junction intermediate in Cre-loxP site-specific recombination.
J.Biol.Chem., 280:8290-8299, 2005

PubMed Abstract: Cre recombinase is a prototypical member of the tyrosine recombinase family of site-specific recombinases. Members of this family of enzymes catalyze recombination between specific DNA sequences by cleaving and exchanging one pair of strands between the two substrate sites to form a 4-way Holliday junction (HJ) intermediate and then resolve the HJ intermediate to recombinant products by a second round of strand exchanges. Recently, hexapeptide inhibitors have been described that are capable of blocking the second strand exchange step in the tyrosine recombinase recombination pathway, leading to an accumulation of the HJ intermediate. These peptides are active in the lambda-integrase, Cre recombinase, and Flp recombinase systems and are potentially important tools for both in vitro mechanistic studies and as in vivo probes of cellular function. Here we present biochemical and crystallographic data that support a model where the peptide inhibitor binds in the center of the recombinase-bound DNA junction and interacts with solvent-exposed bases near the junction branch point. Peptide binding induces large conformational changes in the DNA strands of the HJ intermediate, which affect the active site geometries in the recombinase subunits.

PubMed: 15591069
DOI: 10.1074/jbc.M411668200

実験手法

X-RAY DIFFRACTION (2 Å)