5F4H

Archael RuvB-like Holiday junction helicase

Summary for 5F4H

• Entry DOI: 10.2210/pdb5f4h/pdb
• Descriptor: Nucleotide binding protein PINc, GLYCEROL, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: helicase, atpase, holiday junction, hydrolase
• Biological source: Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)
• Total number of polymer chains: 6
• Total formula weight: 346027.45

Authors

Zhai, B.,DuPrez, K.T.,Doukov, T.I.,Shen, Y.,Fan, L. (deposition date: 2015-12-03, release date: 2016-12-21, Last modification date: 2024-10-23)

Primary citation

Zhai, B.,DuPrez, K.,Doukov, T.I.,Li, H.,Huang, M.,Shang, G.,Ni, J.,Gu, L.,Shen, Y.,Fan, L.
Structure and Function of a Novel ATPase that Interacts with Holliday Junction Resolvase Hjc and Promotes Branch Migration.
J. Mol. Biol., 429:1009-1029, 2017

PubMed Abstract: Holliday junction (HJ) is a hallmark intermediate in DNA recombination and must be processed by dissolution (for double HJ) or resolution to ensure genome stability. Although HJ resolvases have been identified in all domains of life, there is a long-standing effort to search in prokaryotes and eukarya for proteins promoting HJ migration. Here, we report the structural and functional characterization of a novel ATPase, Sulfolobus islandicusPilT N-terminal-domain-containing ATPase (SisPINA), encoded by the gene adjacent to the resolvase Hjc coding gene. PINA is conserved in archaea and vital for S. islandicus viability. Purified SisPINA forms hexameric rings in the crystalline state and in solution, similar to the HJ migration helicase RuvB in Gram-negative bacteria. Structural analysis suggests that ATP binding and hydrolysis cause conformational changes in SisPINA to drive branch migration. Further studies reveal that SisPINA interacts with SisHjc and coordinates HJ migration and cleavage.

PubMed: 28238763
DOI: 10.1016/j.jmb.2017.02.016

Experimental method

X-RAY DIFFRACTION (2.699 Å)