6g7e

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'''Unreleased structure'''
 
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The entry 6g7e is ON HOLD until Paper Publication
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==Crystal structure of Chaetomium thermophilum Mot1 (E1434Q, 1837-1886 deletion mutant)==
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<StructureSection load='6g7e' size='340' side='right' caption='[[6g7e]], [[Resolution|resolution]] 3.21&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6g7e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G7E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G7E FirstGlance]. <br>
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</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>
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<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=6g7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g7e OCA], [http://pdbe.org/6g7e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g7e RCSB], [http://www.ebi.ac.uk/pdbsum/6g7e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g7e ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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 Chaetomium thermophilum. 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.
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Authors:
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Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state.,Butryn A, Woike S, Shetty SJ, Auble DT, Hopfner KP Elife. 2018 Oct 5;7. pii: 37774. doi: 10.7554/eLife.37774. PMID:30289385<ref>PMID:30289385</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6g7e" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Butryn, A]]
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[[Category: Hopfner, K P]]
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[[Category: Atpase]]
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[[Category: Hydrolase]]
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[[Category: Transcription]]

Revision as of 08:06, 17 October 2018

Crystal structure of Chaetomium thermophilum Mot1 (E1434Q, 1837-1886 deletion mutant)

6g7e, resolution 3.21Å

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