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Article

Structure-function analysis of the three domains of RuvB DNA motor protein.

The Journal of biological chemistry - 26 Aug 2005

Ohnishi Takayuki, Hishida Takashi, Harada Yoshie, Iwasaki Hiroshi, Shinagawa Hideo

Abstract excerpt

RuvB protein forms two hexameric rings that bind to the RuvA tetramer at DNA Holliday junctions. The RuvAB complex utilizes the energy of ATP hydrolysis to promote branch migration of Holliday junctions. The crystal structure of RuvB from Thermus thermophilus (Tth) HB8 showed that each RuvB monomer has three domains (N, M, and C). This study is a structure-function analysis of the three domains of RuvB. The...

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Identifiers

PMID: 15972826
DOI: 10.1074/jbc.M502400200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Structure-function analysis of the three domains of RuvB DNA motor protein.PMID 15972826Read ↗

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