6q6e
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural and functional insights into the condensin ATPase cycle== | |
| + | <StructureSection load='6q6e' size='340' side='right'caption='[[6q6e]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6q6e]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q6E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q6E FirstGlance]. <br> | ||
| + | </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=6q6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q6e OCA], [http://pdbe.org/6q6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q6e RCSB], [http://www.ebi.ac.uk/pdbsum/6q6e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q6e ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/G0SBJ6_CHATD G0SBJ6_CHATD]] Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes.[PIRNR:PIRNR017126] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 6q6e" style="background-color:#fffaf0;"></div> |
| - | [[Category: Haering, C | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Haering, C H]] | ||
[[Category: Hassler, M]] | [[Category: Hassler, M]] | ||
[[Category: Hennig, J]] | [[Category: Hennig, J]] | ||
| + | [[Category: Simon, B]] | ||
| + | [[Category: Cohesin]] | ||
| + | [[Category: Condensin]] | ||
| + | [[Category: Smc protein complex]] | ||
| + | [[Category: Structural protein]] | ||
Revision as of 06:00, 3 July 2019
Structural and functional insights into the condensin ATPase cycle
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