View source for 4wzs


==Crystal structure of the Mot1 N-terminal domain in complex with TBP and NC2 bound to a promoter DNA fragment==
<StructureSection load='4wzs' size='340' side='right'caption='[[4wzs]], [[Resolution|resolution]] 3.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4wzs]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Encephalitozoon_cuniculi Encephalitozoon cuniculi], [https://en.wikipedia.org/wiki/Encephalitozoon_cuniculi_GB-M1 Encephalitozoon cuniculi GB-M1] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WZS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WZS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.78&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wzs OCA], [https://pdbe.org/4wzs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wzs RCSB], [https://www.ebi.ac.uk/pdbsum/4wzs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wzs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8SQT6_ENCCU Q8SQT6_ENCCU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1.,Butryn A, Schuller JM, Stoehr G, Runge-Wollmann P, Forster F, Auble DT, Hopfner KP Elife. 2015 Aug 10;4. doi: 10.7554/eLife.07432. PMID:26258880<ref>PMID:26258880</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4wzs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Encephalitozoon cuniculi]]
[[Category: Encephalitozoon cuniculi GB-M1]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Butryn A]]
[[Category: Hopfner K-P]]