EMD-10951

Single-particle
7.5 Å
EMD-10951 Deposition: 28/04/2020
Map released: 15/07/2020
Last modified: 22/05/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-10951

Condensin complex from S.cerevisiae ATP-free apo non-engaged state: overall map

EMD-10951

Single-particle
7.5 Å
EMD-10951 Deposition: 28/04/2020
Map released: 15/07/2020
Last modified: 22/05/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Sample: Condensin
Fitted models: 6yvu (Avg. Q-score: 0.175)

Deposition Authors: Lee B-G, Cawood C , Gutierrez-Escribano P , Nakane T , Merkel F , Hassler M , Haering CH , Aragon L , Lowe J
Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism.
PUBMED: 32661420
DOI: doi:10.1038/s41594-020-0457-x
ISSN: 1545-9985
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.