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X-ray (3.78 Å)
Crystal structure of the mot1 n-terminal domain in complex with tbp and nc2 bound to a promoter DNA fragment
Butryn A, Schuller JM, Stoehr G, Runge-Wollmann P, Forster F, Auble DT, Hopfner KP (2015): "Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1." Elife, 4. doi: 10.7554/eLife.07432.
Swi2/Snf2 ATPases remodel substrates such as nucleosomes and transcription complexes to control a wide range of DNA associated processes, but detailed structural information on the ATP-dependent remodeling reactions is largely absent. The single subunit remodeler Mot1 dissociates TATA box-binding protein (TBP):DNA complexes, offering a useful system to address the structural mechanisms of Swi2/Snf2 ATPases. Here we report the crystal structure of the N-terminal domain of Mot1 in complex with TBP, DNA, and the transcription regulator NC2. Our data show that Mot1 reduces DNA:NC2 interactions and unbends DNA as compared to the TBP:DNA:NC2 state, suggesting that Mot1 primes TBP:NC2 displacement in an ATP-independent manner. Electron microscopy and cross-linking data suggest that the Swi2/Snf2 domain of Mot1 associates with the upstream DNA and the histone fold of NC2, thereby revealing parallels to some nucleosome remodelers. This study provides a structural framework for how a Swi2/Snf2 ATPase interacts with its substrate DNA:protein complex.

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