6ZZ6

Cryo-EM structure of S.cerevisiae cohesin-Scc2-DNA complex

Summary for 6ZZ6

• Entry DOI: 10.2210/pdb6zz6/pdb
• EMDB information: 11585
• Descriptor: Structural maintenance of chromosomes protein 1,Structural maintenance of chromosomes protein 1,Structural maintenance of chromosomes protein 1, Structural maintenance of chromosomes protein 3,Structural maintenance of chromosomes protein 3,Structural maintenance of chromosomes protein 3, Sister chromatid cohesion protein 1,Sister chromatid cohesion protein 1,Sister chromatid cohesion protein 1, ... (8 entities in total)
• Functional Keywords: smc, cohesin, dna, cell cycle
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 6
• Total formula weight: 291548.38

Authors

Lee, B.-G.,Gonzalez Llamazares, A.,Collier, J.,Nasmyth, K.A.,Lowe, J. (deposition date: 2020-08-04, release date: 2020-09-30, Last modification date: 2024-05-01)

Primary citation

Collier, J.E.,Lee, B.G.,Roig, M.B.,Yatskevich, S.,Petela, N.J.,Metson, J.,Voulgaris, M.,Gonzalez Llamazares, A.,Lowe, J.,Nasmyth, K.A.
Transport of DNA within cohesin involves clamping on top of engaged heads by Scc2 and entrapment within the ring by Scc3.
Elife, 9:-, 2020

PubMed Abstract: In addition to extruding DNA loops, cohesin entraps within its SMC-kleisin ring (S-K) individual DNAs during G1 and sister DNAs during S-phase. All three activities require related hook-shaped proteins called Scc2 and Scc3. Using thiol-specific crosslinking we provide rigorous proof of entrapment activity in vitro. Scc2 alone promotes entrapment of DNAs in the E-S and E-K compartments, between ATP-bound engaged heads and the SMC hinge and associated kleisin, respectively. This does not require ATP hydrolysis nor is it accompanied by entrapment within S-K rings, which is a slower process requiring Scc3. Cryo-EM reveals that DNAs transported into E-S/E-K compartments are 'clamped' in a sub-compartment created by Scc2's association with engaged heads whose coiled coils are folded around their elbow. We suggest that clamping may be a recurrent feature of cohesin complexes active in loop extrusion and that this conformation precedes the S-K entrapment required for sister chromatid cohesion.

PubMed: 32930661
DOI: 10.7554/eLife.59560

Experimental method

ELECTRON MICROSCOPY (3.4 Å)