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• W2895026368 abstract "Swi2/Snf2 ATPases remodel protein:DNA complexes in all of the fundamental chromosome-associated processes. The single-subunit remodeler Mot1 dissociates TATA box-binding protein (TBP):DNA complexes and provides a simple model for obtaining structural insights into the action of Swi2/Snf2 ATPases. Previously we reported how the N-terminal domain of Mot1 binds TBP, NC2 and DNA, but the location of the C-terminal ATPase domain remained unclear (<xref ref-type=bibr rid=bib8>Butryn et al., 2015</xref>). Here, we report the crystal structure of the near full-length Mot1 from Chaetomium thermophilum. Our data show that Mot1 adopts a ring like structure with a catalytically inactive resting state of the ATPase. Biochemical analysis suggests that TBP binding switches Mot1 into an ATP hydrolysis-competent conformation. Combined with our previous results, these data significantly improve the structural model for the complete Mot1:TBP:DNA complex and suggest a general mechanism for Mot1 action." @default.
• W2895026368 created "2018-10-12" @default.
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• W2895026368 date "2018-10-05" @default.
• W2895026368 modified "2023-10-17" @default.
• W2895026368 title "Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state" @default.
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• W2895026368 doi "https://doi.org/10.7554/elife.37774" @default.
• W2895026368 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6188472" @default.
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• W2895026368 hasPublicationYear "2018" @default.
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