Crystal structure of the left-handed archaeal RadA helical filament: Identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins

Li Tzu Chen, Tzu Ping Ko, Yuan Chih Chang, Kuei An Lin, Chia Seng Chang, Andrew H.J. Wang, Ting Fang Wang

研究成果: 雜誌貢獻文章同行評審

35 引文 斯高帕斯(Scopus)

摘要

The RecA family of proteins mediates homologous recombination, an evolutionarily conserved pathway that maintains genomic stability by protecting against DNA double strand breaks. RecA proteins are thought to facilitate DNA strand exchange reactions as closed-rings or as right-handed helical filaments. Here, we report the crystal structure of a left-handed Sulfolobus solfataricus RadA helical filament. Each protomer in this left-handed filament is linked to its neighbour via interactions of a b-strand polymerization motif with the neighbouring ATPase domain. Immediately following the polymerization motif, we identified an evolutionarily conserved hinge region (a subunit rotation motif) in which a 3608 clockwise axial rotation accompanies stepwise structural transitions from a closed ring to the AMP-PNP right-handed filament, then to an overwound right-handed filament and finally to the left-handed filament. Additional structural and functional analyses of wild-type and mutant proteins confirmed that the subunit rotation motif is crucial for enzymatic functions of RecA family proteins. These observations support the hypothesis that RecA family protein filaments may function as rotary motors.

原文英語
頁(從 - 到)1787-1801
頁數15
期刊Nucleic Acids Research
35
發行號6
DOIs
出版狀態已發佈 - 3月 2007
對外發佈

ASJC Scopus subject areas

  • 遺傳學

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