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7Z8S

Mot1:TBP:DNA - post hydrolysis state

Summary for 7Z8S
Entry DOI10.2210/pdb7z8s/pdb
EMDB information14562
DescriptorDNA (36-MER), Putative tata-box binding protein, Helicase-like protein, ... (4 entities in total)
Functional Keywordsswi2/snf2 protein, remodeler, transcription initiation, transcription
Biological sourceChaetomium thermophilum
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Total number of polymer chains4
Total formula weight263672.80
Authors
Woike, S.,Eustermann, S.,Jung, J.,Wenzl, S.J.,Hagemann, G.,Bartho, J.D.,Lammens, K.,Butryn, A.,Herzog, F.,Hopfner, K.-P. (deposition date: 2022-03-18, release date: 2023-03-29, Last modification date: 2024-07-24)
Primary citationWoike, S.,Eustermann, S.,Jung, J.,Wenzl, S.J.,Hagemann, G.,Bartho, J.,Lammens, K.,Butryn, A.,Herzog, F.,Hopfner, K.P.
Structural basis for TBP displacement from TATA box DNA by the Swi2/Snf2 ATPase Mot1.
Nat.Struct.Mol.Biol., 30:640-649, 2023
Cited by
PubMed Abstract: The Swi2/Snf2 family transcription regulator Modifier of Transcription 1 (Mot1) uses adenosine triphosphate (ATP) to dissociate and reallocate the TATA box-binding protein (TBP) from and between promoters. To reveal how Mot1 removes TBP from TATA box DNA, we determined cryogenic electron microscopy structures that capture different states of the remodeling reaction. The resulting molecular video reveals how Mot1 dissociates TBP in a process that, intriguingly, does not require DNA groove tracking. Instead, the motor grips DNA in the presence of ATP and swings back after ATP hydrolysis, moving TBP to a thermodynamically less stable position on DNA. Dislodged TBP is trapped by a chaperone element that blocks TBP's DNA binding site. Our results show how Swi2/Snf2 proteins can remodel protein-DNA complexes through DNA bending without processive DNA tracking and reveal mechanistic similarities to RNA gripping DEAD box helicases and RIG-I-like immune sensors.
PubMed: 37106137
DOI: 10.1038/s41594-023-00966-0
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.9 Å)
Structure validation

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