7CQ2

Crystal structure of Slx1-Slx4

7CQ2 の概要

• エントリーDOI: 10.2210/pdb7cq2/pdb
• 分子名称: Structure-specific endonuclease subunit SLX1, SLX4 isoform 1, ZINC ION, ... (5 entities in total)
• 機能のキーワード: endonuclease complex, holliday junction, slx1-slx4, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (strain YJM789) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 106277.74

構造登録者

Xu, X.,Wang, M.,Sun, J.,Li, G.,Yang, N.,Xu, R.M. (登録日: 2020-08-08, 公開日: 2021-06-16, 最終更新日: 2024-05-29)

主引用文献

Xu, X.,Wang, M.,Sun, J.,Yu, Z.,Li, G.,Yang, N.,Xu, R.M.
Structure specific DNA recognition by the SLX1-SLX4 endonuclease complex.
Nucleic Acids Res., 49:7740-7752, 2021

PubMed Abstract: The SLX1-SLX4 structure-specific endonuclease complex is involved in processing diverse DNA damage intermediates, including resolution of Holliday junctions, collapse of stalled replication forks and removal of DNA flaps. The nuclease subunit SLX1 is inactive on its own, but become activated upon binding to SLX4 via its conserved C-terminal domain (CCD). Yet, how the SLX1-SLX4 complex recognizes specific DNA structure and chooses cleavage sites remains unknown. Here we show, through a combination of structural, biochemical and computational analyses, that the SAP domain of SLX4 is critical for efficient and accurate processing of 5'-flap DNA. It binds the minor groove of DNA about one turn away from the flap junction, and the 5'-flap is implicated in binding the core domain of SLX1. This binding mode accounts for specific recognition of 5'-flap DNA and specification of cleavage site by the SLX1-SLX4 complex.

PubMed: 34181713
DOI: 10.1093/nar/gkab542

実験手法

X-RAY DIFFRACTION (2.5 Å)