6YUF

Cohesin complex with loader gripping DNA

Summary for 6YUF

• Entry DOI: 10.2210/pdb6yuf/pdb
• EMDB information: 10930
• Descriptor: Cohesin subunit rad21, Sister chromatid cohesion protein mis4, Structural maintenance of chromosomes protein 1, ... (8 entities in total)
• Functional Keywords: chromosome segregation sister chromatid cohesion smc complexes cohesin abc-atpase mis4-scc2-nipbl, dna binding protein
• Biological source: Schizosaccharomyces pombe (strain 972 / ATCC 24843); More
• Total number of polymer chains: 6
• Total formula weight: 547283.87

Authors

Higashi, T.L.,Eickhoff, P.,Sousa, J.S.,Costa, A.,Uhlmann, F. (deposition date: 2020-04-27, release date: 2020-08-19, Last modification date: 2025-07-09)

Primary citation

Higashi, T.L.,Eickhoff, P.,Sousa, J.S.,Locke, J.,Nans, A.,Flynn, H.R.,Snijders, A.P.,Papageorgiou, G.,O'Reilly, N.,Chen, Z.A.,O'Reilly, F.J.,Rappsilber, J.,Costa, A.,Uhlmann, F.
A Structure-Based Mechanism for DNA Entry into the Cohesin Ring.
Mol.Cell, 79:917-, 2020

PubMed Abstract: Despite key roles in sister chromatid cohesion and chromosome organization, the mechanism by which cohesin rings are loaded onto DNA is still unknown. Here we combine biochemical approaches and cryoelectron microscopy (cryo-EM) to visualize a cohesin loading intermediate in which DNA is locked between two gates that lead into the cohesin ring. Building on this structural framework, we design experiments to establish the order of events during cohesin loading. In an initial step, DNA traverses an N-terminal kleisin gate that is first opened upon ATP binding and then closed as the cohesin loader locks the DNA against the ATPase gate. ATP hydrolysis will lead to ATPase gate opening to complete DNA entry. Whether DNA loading is successful or results in loop extrusion might be dictated by a conserved kleisin N-terminal tail that guides the DNA through the kleisin gate. Our results establish the molecular basis for cohesin loading onto DNA.

PubMed: 32755595
DOI: 10.1016/j.molcel.2020.07.013

Experimental method

ELECTRON MICROSCOPY (3.94 Å)