6g7e: Difference between revisions
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==Crystal structure of Chaetomium thermophilum Mot1 (E1434Q, 1837-1886 deletion mutant)== | |||
<StructureSection load='6g7e' size='340' side='right' caption='[[6g7e]], [[Resolution|resolution]] 3.21Å' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</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=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> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6g7e" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Butryn, A]] | |||
[[Category: Hopfner, K P]] | |||
[[Category: Atpase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Transcription]] | |||
Revision as of 08:06, 17 October 2018
Crystal structure of Chaetomium thermophilum Mot1 (E1434Q, 1837-1886 deletion mutant)
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