5YWW

Archael RuvB-like Holiday junction helicase

5YWW の概要

• エントリーDOI: 10.2210/pdb5yww/pdb
• 関連するPDBエントリー: 5F4H
• 分子名称: Nucleotide binding protein PINc, GLYCEROL (3 entities in total)
• 機能のキーワード: atpase, helicase, hydrolase
• 由来する生物種: Sulfolobus islandicus REY15A
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57245.11

構造登録者

Zhai, B.,Yuan, Z.,Han, X.,DuPrez, K.,Shen, Y.,Fan, L. (登録日: 2017-11-30, 公開日: 2018-06-13, 最終更新日: 2023-11-22)

主引用文献

Zhai, B.,DuPrez, K.,Han, X.,Yuan, Z.,Ahmad, S.,Xu, C.,Gu, L.,Ni, J.,Fan, L.,Shen, Y.
The archaeal ATPase PINA interacts with the helicase Hjm via its carboxyl terminal KH domain remodeling and processing replication fork and Holliday junction.
Nucleic Acids Res., 46:6627-6641, 2018

PubMed Abstract: PINA is a novel ATPase and DNA helicase highly conserved in Archaea, the third domain of life. The PINA from Sulfolobus islandicus (SisPINA) forms a hexameric ring in crystal and solution. The protein is able to promote Holliday junction (HJ) migration and physically and functionally interacts with Hjc, the HJ specific endonuclease. Here, we show that SisPINA has direct physical interaction with Hjm (Hel308a), a helicase presumably targeting replication forks. In vitro biochemical analysis revealed that Hjm, Hjc, and SisPINA are able to coordinate HJ migration and cleavage in a concerted way. Deletion of the carboxyl 13 amino acid residues impaired the interaction between SisPINA and Hjm. Crystal structure analysis showed that the carboxyl 70 amino acid residues fold into a type II KH domain which, in other proteins, functions in binding RNA or ssDNA. The KH domain not only mediates the interactions of PINA with Hjm and Hjc but also regulates the hexameric assembly of PINA. Our results collectively suggest that SisPINA, Hjm and Hjc work together to function in replication fork regression, HJ formation and HJ cleavage.

PubMed: 29846688
DOI: 10.1093/nar/gky451

実験手法

X-RAY DIFFRACTION (2.33 Å)