6YVD

Head segment of the S.cerevisiae condensin holocomplex in presence of ATP

Summary for 6YVD

• Entry DOI: 10.2210/pdb6yvd/pdb
• EMDB information: 10944
• Descriptor: Condensin complex subunit 2, Condensin complex subunit 3, Structural maintenance of chromosomes protein 2, ... (4 entities in total)
• Functional Keywords: condensin chromosome condensation smc protein, cell cycle
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c); More
• Total number of polymer chains: 4
• Total formula weight: 513029.66

Authors

Merkel, F.,Haering, C.H.,Hassler, M.,Lee, B.G.,Lowe, J. (deposition date: 2020-04-28, release date: 2020-07-22, Last modification date: 2024-07-10)

Primary citation

Lee, B.G.,Merkel, F.,Allegretti, M.,Hassler, M.,Cawood, C.,Lecomte, L.,O'Reilly, F.J.,Sinn, L.R.,Gutierrez-Escribano, P.,Kschonsak, M.,Bravo, S.,Nakane, T.,Rappsilber, J.,Aragon, L.,Beck, M.,Lowe, J.,Haering, C.H.
Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism.
Nat.Struct.Mol.Biol., 27:743-751, 2020

PubMed Abstract: 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.

PubMed: 32661420
DOI: 10.1038/s41594-020-0457-x

Experimental method

ELECTRON MICROSCOPY (7.6 Å)