4wzs
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==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]] 3.78Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4wzs]] is a 6 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WZS FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wzs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wzs RCSB], [http://www.ebi.ac.uk/pdbsum/4wzs PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Butryn, A]] | [[Category: Butryn, A]] | ||
| + | [[Category: Hopfner, K P]] | ||
| + | [[Category: Protein-dna complex]] | ||
| + | [[Category: Swi2/snf2]] | ||
| + | [[Category: Transcription]] | ||
Revision as of 13:30, 26 August 2015
Crystal structure of the Mot1 N-terminal domain in complex with TBP and NC2 bound to a promoter DNA fragment
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