5YWW

Archael RuvB-like Holiday junction helicase

Summary for 5YWW

• Entry DOI: 10.2210/pdb5yww/pdb
• Related: 5F4H
• Descriptor: Nucleotide binding protein PINc, GLYCEROL (3 entities in total)
• Functional Keywords: atpase, helicase, hydrolase
• Biological source: Sulfolobus islandicus REY15A
• Total number of polymer chains: 1
• Total formula weight: 57245.11

Authors

Zhai, B.,Yuan, Z.,Han, X.,DuPrez, K.,Shen, Y.,Fan, L. (deposition date: 2017-11-30, release date: 2018-06-13, Last modification date: 2023-11-22)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.33 Å)