6G7E
Crystal structure of Chaetomium thermophilum Mot1 (E1434Q, 1837-1886 deletion mutant)
Summary for 6G7E
| Entry DOI | 10.2210/pdb6g7e/pdb |
| Descriptor | Helicase-like protein (1 entity in total) |
| Functional Keywords | atpase, hydrolase, transcription |
| Biological source | Chaetomium thermophilum var. thermophilum DSM 1495 |
| Total number of polymer chains | 1 |
| Total formula weight | 209128.02 |
| Authors | Butryn, A.,Hopfner, K.-P. (deposition date: 2018-04-05, release date: 2018-10-17, Last modification date: 2024-10-23) |
| Primary citation | Butryn, A.,Woike, S.,Shetty, S.J.,Auble, D.T.,Hopfner, K.P. Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state. Elife, 7:-, 2018 Cited by PubMed 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 (Butryn et al., 2015). Here, we report the crystal structure of the near full-length Mot1 from 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. PubMed: 30289385DOI: 10.7554/eLife.37774 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2129 Å) |
Structure validation
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