6qj1

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m (Protected "6qj1" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6qj1 is ON HOLD until Paper Publication
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==Crystal structure of the C. thermophilum condensin Smc2 ATPase head (crystal from I)==
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<StructureSection load='6qj1' size='340' side='right'caption='[[6qj1]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6qj1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QJ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QJ1 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=6qj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qj1 OCA], [http://pdbe.org/6qj1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qj1 RCSB], [http://www.ebi.ac.uk/pdbsum/6qj1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qj1 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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The condensin protein complex plays a key role in the structural organization of genomes. How the ATPase activity of its SMC subunits drives large-scale changes in chromosome topology has remained unknown. Here we reconstruct, at near-atomic resolution, the sequence of events that take place during the condensin ATPase cycle. We show that ATP binding induces a conformational switch in the Smc4 head domain that releases its hitherto undescribed interaction with the Ycs4 HEAT-repeat subunit and promotes its engagement with the Smc2 head into an asymmetric heterodimer. SMC head dimerization subsequently enables nucleotide binding at the second active site and disengages the Brn1 kleisin subunit from the Smc2 coiled coil to open the condensin ring. These large-scale transitions in the condensin architecture lay out a mechanistic path for its ability to extrude DNA helices into large loop structures.
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Authors:
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Structural Basis of an Asymmetric Condensin ATPase Cycle.,Hassler M, Shaltiel IA, Kschonsak M, Simon B, Merkel F, Tharichen L, Bailey HJ, Macosek J, Bravo S, Metz J, Hennig J, Haering CH Mol Cell. 2019 Jun 20;74(6):1175-1188.e9. doi: 10.1016/j.molcel.2019.03.037. PMID:31226277<ref>PMID:31226277</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 6qj1" 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: Large Structures]]
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[[Category: Haering, C H]]
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[[Category: Hassler, M]]
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[[Category: Cell cycle]]
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[[Category: Condensin smc complex atpase chromosome condensation loop extrusion]]

Revision as of 06:00, 3 July 2019

Crystal structure of the C. thermophilum condensin Smc2 ATPase head (crystal from I)

PDB ID 6qj1

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