4WZS

Crystal structure of the Mot1 N-terminal domain in complex with TBP and NC2 bound to a promoter DNA fragment

Summary for 4WZS

• Entry DOI: 10.2210/pdb4wzs/pdb
• Descriptor: ECU11_1470 protein, TATA-binding protein-associated phosphoprotein, Similarity to HELICASE MOT1, ... (6 entities in total)
• Functional Keywords: transcription, protein-dna complex, swi2/snf2
• Biological source: Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite); More
• Cellular location: Nucleus : M1K2J7
• Total number of polymer chains: 6
• Total formula weight: 156813.95

Authors

Butryn, A.,Hopfner, K.-P. (deposition date: 2014-11-20, release date: 2015-08-26, Last modification date: 2024-11-06)

Primary citation

Butryn, A.,Schuller, J.M.,Stoehr, G.,Runge-Wollmann, P.,Forster, F.,Auble, D.T.,Hopfner, K.P.
Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1.
Elife, 4:-, 2015

PubMed Abstract: 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 (modifier of transcription 1) 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 negative cofactor 2 (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.

PubMed: 26258880
DOI: 10.7554/eLife.07432

Experimental method

X-RAY DIFFRACTION (3.78 Å)