6yvv: Difference between revisions
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==Condensin complex from S.cerevisiae ATP-free apo bridged state== | |||
<StructureSection load='6yvv' size='340' side='right'caption='[[6yvv]], [[Resolution|resolution]] 7.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6yvv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YVV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YVV FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.5Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6yvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yvv OCA], [https://pdbe.org/6yvv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yvv RCSB], [https://www.ebi.ac.uk/pdbsum/6yvv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yvv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SMC2_YEAST SMC2_YEAST] Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Complexes containing a pair of structural maintenance of chromosomes (SMC) family proteins are fundamental for the three-dimensional (3D) organization of genomes in all domains of life. The eukaryotic SMC complexes cohesin and condensin are thought to fold interphase and mitotic chromosomes, respectively, into large loop domains, although the underlying molecular mechanisms have remained unknown. We used cryo-EM to investigate the nucleotide-driven reaction cycle of condensin from the budding yeast Saccharomyces cerevisiae. Our structures of the five-subunit condensin holo complex at different functional stages suggest that ATP binding induces the transition of the SMC coiled coils from a folded-rod conformation into a more open architecture. ATP binding simultaneously triggers the exchange of the two HEAT-repeat subunits bound to the SMC ATPase head domains. We propose that these steps result in the interconversion of DNA-binding sites in the catalytic core of condensin, forming the basis of the DNA translocation and loop-extrusion activities. | |||
Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism.,Lee BG, Merkel F, Allegretti M, Hassler M, Cawood C, Lecomte L, O'Reilly FJ, Sinn LR, Gutierrez-Escribano P, Kschonsak M, Bravo S, Nakane T, Rappsilber J, Aragon L, Beck M, Lowe J, Haering CH Nat Struct Mol Biol. 2020 Jul 13. pii: 10.1038/s41594-020-0457-x. doi:, 10.1038/s41594-020-0457-x. PMID:32661420<ref>PMID:32661420</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6yvv" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae S288C]] | |||
[[Category: Aragon L]] | |||
[[Category: Cawood C]] | |||
[[Category: Gutierrez-Escribano P]] | |||
[[Category: Haering CH]] | |||
[[Category: Hassler M]] | |||
[[Category: Lee B-G]] | |||
[[Category: Lowe J]] | |||
[[Category: Merkel F]] | |||
[[Category: Nakane T]] |
Latest revision as of 13:22, 22 May 2024
Condensin complex from S.cerevisiae ATP-free apo bridged stateCondensin complex from S.cerevisiae ATP-free apo bridged state
Structural highlights
FunctionSMC2_YEAST Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. Publication Abstract from PubMedComplexes containing a pair of structural maintenance of chromosomes (SMC) family proteins are fundamental for the three-dimensional (3D) organization of genomes in all domains of life. The eukaryotic SMC complexes cohesin and condensin are thought to fold interphase and mitotic chromosomes, respectively, into large loop domains, although the underlying molecular mechanisms have remained unknown. We used cryo-EM to investigate the nucleotide-driven reaction cycle of condensin from the budding yeast Saccharomyces cerevisiae. Our structures of the five-subunit condensin holo complex at different functional stages suggest that ATP binding induces the transition of the SMC coiled coils from a folded-rod conformation into a more open architecture. ATP binding simultaneously triggers the exchange of the two HEAT-repeat subunits bound to the SMC ATPase head domains. We propose that these steps result in the interconversion of DNA-binding sites in the catalytic core of condensin, forming the basis of the DNA translocation and loop-extrusion activities. Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism.,Lee BG, Merkel F, Allegretti M, Hassler M, Cawood C, Lecomte L, O'Reilly FJ, Sinn LR, Gutierrez-Escribano P, Kschonsak M, Bravo S, Nakane T, Rappsilber J, Aragon L, Beck M, Lowe J, Haering CH Nat Struct Mol Biol. 2020 Jul 13. pii: 10.1038/s41594-020-0457-x. doi:, 10.1038/s41594-020-0457-x. PMID:32661420[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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